Structures of substrate binding pockets of SCF complexes

ABSTRACT

The present invention relates to binding pockets of Skp1-Cdc53/Cullin-F-box protein (SCF) E3 ubiquitin ligases associated with substrate selection and/or orientation. In particular, the invention relates to a crystal comprising such binding pockets. The crystal may be useful for modeling and/or synthesizing mimetics of a binding pocket or ligands that associate with the binding pocket. Such mimetics or ligands may be capable of acting as modulators of the interactions of a SCF E3 ubiquitin ligase and its substrates, and they may be useful for treating, inhibiting, or preventing diseases modulated by such interactions. Methods are also provided for regulating a SCF E3 ubiquitin ligase comprising changing a binding pocket associated with substrate selection and/or orientation.

[0001] A portion of the disclosure of this patent document contains material that is subject to copyright protection. The copyright owner has no objection to the facsimile reproduction by anyone of the patent document or patent disclosure, as it appears in the Patent and Trademark Office patent file or records, but otherwise reserves all copyright rights whatsoever.

FIELD OF THE INVENTION

[0002] The present invention relates to binding pockets of Skp1-Cdc53/Cullin-F-box protein (SCF) E3 ubiquitin ligases associated with substrate selection and/or orientation. In particular, the invention relates to a crystal comprising such binding pockets. The crystal may be useful for modeling and/or synthesizing mimetics of a binding pocket or ligands that associate with the binding pocket. Such mimetics or ligands may be capable of acting as modulators of the interactions of an SCF E3 ubiquitin ligase and its substrates, and they may be useful for treating, inhibiting, or preventing diseases modulated by such interactions.

[0003] Methods are also provided for regulating an SCF E3 ubiquitin ligase comprising changing a binding pocket associated with substrate selection and/or orientation.

BACKGROUND

[0004] The ubiquitin proteolytic system controls the precisely timed degradation of regulatory proteins in signaling, development and cell cycle progression. Substrate ubiquitination is catalyzed by a cascade of enzymes, termed E1, E2 and E3, which activate and then conjugate ubiquitin to the substrate (Hershko and Ciechanover, 1998). E3 enzymes, also known as ubiquitin ligases, contain substrate-specific recognition domains and catalyze the final step in ubiquitin transfer. Recognition is mediated by primary sequence elements in the substrate, referred to as degrons (Varshavsky, 1991). Control of the E3-substrate interaction forms the basis for regulated proteolysis; often post-translational substrate modification, most commonly phosphorylation, serves to target substrates to their cognate E3 enzymes (Deshaies, 1999). Two main classes of E3 enzyme are now evident, as characterized by the presence of either a HECT domain or a RING domain. The HECT domain class forms a catalytically essential thioester with ubiquitin, whereas the RING domain class relies on the E2 enzymes to provide catalytic activity (Pickart, 2001). The RING domain forms an E2 docking site and orients the substrate with respect to the E2.

[0005] Phosphorylation-dependent degrons direct substrates to a recently described class of multisubunit E3 enzymes termed Skp1-Cdc53/Cullin-F-box protein (SCF) complexes. SCF complexes are built on an invariant core machinery comprised of the adapter protein Skp1, the scaffold protein Cdc53 (called Cull in metazoans), and the RING-H2 domain protein Rbx1 (also called Roc1 or Hrt1), which interacts with an E2 enzyme, usually Cdc34 (Pickart, 2001). Substrates are brought to the core complex by one of a large family of variable adapter subunits called F-box proteins, each of which targets a limited number of specific substrates (Bai et al., 1996, Patton et al., 1998). F-box proteins typically have a bipartite structure with an N-terminal ˜40 amino acid F-box motif and a C-terminal protein-protein interaction domain, such as WD40 repeats or leucine rich repeats, which bind substrates (Bai et al, 1996; Feldman et al, 1997; Skowyra et al., 1997). The overall architecture of SCF complexes is conserved in several related ubiquitin ligase complexes including the Anaphase Promoting Complex/Cyclosome and the Von Hippel Lindau (VHL) tumor suppressor protein complex, each of which contain cullin family members, RING-H2 domain and substrate recognition subunits (Pickart, 2001; Kaelin, 2002).

[0006] Cell cycle progression depends on the precisely timed elimination of cyclins and cyclin-dependent kinase (CDK) inhibitors by the ubiquitin system (Harper et al, 2002). In yeast, G1 cyclin CDK activity phosphorylates a CDK inhibitor called Sic1, whose degradation is necessary for onset of B-type cyclin CDK activity and DNA replication (Schwob et al., 1994). Phospho-Sic1 is specifically recognized by the F-box protein Cdc4, which recruits Sic1 for ubiquitination by the Cdc34-SCF complex (Bai et al., 1996; Feldman et al., 1997; Skowyra et al., 1997). Stable forms of Sic1 that lack CDK phosphorylation sites cause a G1 phase arrest (Verma et al., 1997), whereas deletion of SIC1 causes premature DNA replication and rampant genome instability (Lengronne and Schwob, 2002). Cdc4 recruits several other substrates to the SCF core complex in a phosphorylation dependent manner, including the Cln-Cdc28 inhibitor/cytoskeletal scaffold protein Far1, the replication protein Cdc6 and the transcription factor Gcn4 (Patton et al., 1998). The F-box protein Grr1 functions in an analogous manner to render G1 cyclins unstable throughout the cell cycle, in a manner that depends on recognition of phospho-epitopes by the LRR domain of Grr1 (Skowyra et al, 1997; Hsiung et al, 2001).

[0007] In the metazoan cell cycle, SCF complexes target phosphorylated forms of the CDK inhibitor p27^(Kip1) and cyclin E, among other substrates. Interestingly, F-box protein specificity for these substrates is reversed compared to yeast, in that the WD40 domain of hCdc4/Fbw7/Ago/SEL-10 recognizes cyclin E (Strohmaier et al., 2001; Koepp et al., 2001; Moberg et al., 2001), whereas the LRR domain of Skp2 recognizes p27^(Kip1) in conjunction with the CDK-binding protein Cks1 (Harper, 2001). Both of these degradation pathways are perturbed in cancer cells. Many primary tumors express high levels of Skp2, which leads to premature degradation of p27^(Kip1) and cell cycle entry (Harper, 2001). Conversely, loss of Cdc4 function causes deregulation of cyclin E-CDK2 activity, which leads to precocious S phase entry and genome instability (Spruck et al., 1999). Mutations in the Drosophila homolog of CDC4, called ago, were isolated as homozygous recessive alleles in a screen for excess cell proliferation, a defect attributed to ectopic cyclin E activity (Moberg et al., 2001). Mutations in hCDC4 have been detected in several cancer cell lines that exhibit high levels of cyclin E (Moberg et al., 2001; Strohmaier et al., 2001), as well as in a significant fraction of primary endometrial cancers (Spruck et al., 2002). In addition, hCDC4 is located in the 4q32region, which is often deleted in various cancers (Spruck et al., 2002). Significantly, a high level of cyclin E correlates strongly with low survival rates in breast cancer (Keyomarsi et al., 2002). Other important substrates appear to be targeted for degradation by Cdc4 orthologs in a phosphorylation-dependent manner, including actived forms of the developmental regulator Notch and the presenilins, which are implicated in familial early onset Alzheimer's disease (Lai, 2002; Selkoe, 2001). SCF-dependent proteolysis also mediates other important signaling events, including phosphorylation-dependent degradation of the NFκB inhibitor IκBα and the proto-oncogene product β-catenin by the F-box protein β-TrCP (Pickart, 2001).

[0008] Several F-box proteins can recognize short phosphopeptide motifs that correspond to substrate sequences. However, it is unknown whether such interactions are analogous to phosphorylation-dependent interactions of SH2, PTB, 14-3-3, WW and FHA domains, each of which has been crystallized with its cognate phosphopeptide (Yaffe and Elia, 2001). For many SCF substrates, including Sic1, Cdc6 and Cln2, phosphorylation on multiple dispersed sites is required for recognition and degradation (Patton et al., 1998). We recently defined a high affinity consensus phosphopeptide binding motif for Cdc4, termed the Cdc4 phospho-degron (CPD), which bears the consensus I/L-I/L/P-pT-P-<KR>₄ [SEQ ID NO:1], where < > indicates a disallowed residue (Nash et al., 2001). The P0 phospho-threonine residue, or less favorably a phospho-serine residue, and the P+1 proline are essential for interaction with Cdc4. Unexpectedly, the CPD consensus is at odds with the CDK phosphorylation site consensus, S/T-P-X-K/R [SEQ ID NO:2](Endicott et al., 1999). Thus, substrate recognition by the targeting kinase is counter-balanced against the targeting component of the degradation machinery. All nine CPD sites in Sic1 have one or more sub-optimal features: all lack consensus hydrophobic residues in the P−1 or P−2 positions, four have serine in place of threonine in the P0 position, and seven contain a disfavored basic residue in one of the +2 to +5 positions. Unexpectedly, Sic1 must be phosphorylated on at least six of its nine sites in order to allow recognition by Cdc4 (Nash et al., 2001). This requirement for multi-site phosphorylation in principle renders the rate of Sic1 degradation proportional to the sixth power of G1 CDK concentration (Ferrell, 1996). The inherently ultrasensitive nature of the Sic1 degradation reaction appears critical for the coordinated initiation of DNA replication by S phase CDK activity (Nash et al., 2001; Lengronne and Schwob, 2002).

[0009] The mechanism of the ubiquitin conjugation reaction is not well understood. The ability of E2-E3 enzyme complexes to form polymers of ubiquitin, itself an 8 kDa protein, on a protein substrate presumably demands a large catalytic cradle simply to accommodate the initial reactants (Pickart, 2001). The sequential addition of ubiquitin moieties onto the substrate must also entail considerable flexibility of the substrate and/or the enzyme complex in order to extend the ubiquitin chain. Recent structure determination and modeling of three E2-E3 complexes has provided insight into these issues. A complex of the E2 enzyme UbCH7 and the HECT domain enzyme E6AP reveals a distance of ˜50 Å between the E2 and E3 active sites, suggesting that catalytic transfer of ubiquitin requires large scale movements in an as yet undefined process (Huang et al., 1999). Similarly, a complex between UbCH7 and the RING domain E3 c-Cb1 contains a substantial gap between the E2 active site and the substrate binding site on c-Cb1 (Zheng et al., 2000). Structures of the SOCS-box adapter protein VHL in complex with a hydroxylated substrate peptide have recently been solved (Kaelin, 2002), but the orientation of the substrate binding site with respect to the E2 enzyme is unknown. Finally, structure determination and molecular modeling of the holo-SCF^(skp2) complex again suggests a distance of ˜50 Å between the substrate binding LRR domain in Skp2 and the E2 active site (Zheng et al., 2002). Notably, the extensive interdigitation of the Skp1-Skp2 interface and the Skp2 inter-domain interface rigidly fixes the orientation of the LRRs of Skp2, suggesting that the F-box protein might hold the substrate in a very precise orientation with respect to the E2 enzyme (Schulman et al., 2000). However, because the substrate binding site on Skp2 has not been determined, either by mutation or by co-crystallization with substrate peptide, it is not possible to deduce how SCF substrates might be positioned with respect to the E2 catalytic site.

SUMMARY OF THE INVENTION

[0010] Applicants have determined the structures of binding pockets of SCF E3 ubiquitin ligases involved in substrate recognition and/or orientation. More particularly, Applicants have solved the x-ray crystal structure of binding pockets of F-box proteins/F-box protein-Skp1 complexes of SCF E3 ubiquitin ligases that interact with Cdc4 phospho-degron (CPD) motifs.

[0011] Solving the crystal structure has enabled the determination of key structural features of substrate binding pockets of a SCF E3 ubiquitin ligase, particularly the shape of binding pockets, or parts thereof, that permit association of a substrate with a SCF E3 ubiquitin ligase or part thereof. The crystal structure also enables the determination of key structural features in substrates or ligands that interact or associate with the binding pockets.

[0012] Knowledge of the structural features of substrate binding pockets of a SCF E3 ubiquitin ligase is of significant utility in drug discovery. The SCF E3 ubiquitin ligase substrate interaction is the basis of many biological mechanisms. In particular it is the basis for regulated ubiquitin proteolysis resulting in degradation of regulatory proteins involved in signaling, development, and cell cycle progression. In addition, drugs may exert their effects through association with the binding pockets of SCF E3 ubiquitin ligases. The associations may occur with all or any parts of a binding pocket. An understanding of the association of a drug with binding pockets of SCF E3 ubiquitin ligases will lead to the design and optimization of drugs having more favorable associations with their targets and thus provide improved biological effects. Therefore, information about the shape and structure of substrate binding pockets of SCF E3 ubiquitin ligases is invaluable in designing potential modulators of the SCF E3 ubiquitin ligases for use in treating diseases and conditions associated with or modulated by the SCF ubiquitin ligases, including cancer and Alzheimer's Disease.

[0013] The present invention relates to an isolated binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation. In an embodiment, the invention relates to a binding pocket of an F-box protein/F-box protein-Skp1 complex of a SCF E3 ubiquitin ligase that interacts with a Cdc4 phospho-degron (CPD) motif. In an aspect of the invention, the binding pocket regulates the binding of a CPD motif to a SCF E3 ubiquitin ligase.

[0014] In an embodiment, the invention comprises the structure of a WD repeat domain of an F-box protein. The structure may also comprise a helical linker of an F-box protein and optionally an F-box domain of an F-box protein. Still further the structure may comprise a Skp1 protein.

[0015] The invention also relates to a crystal comprising a binding pocket of a SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation.

[0016] In an embodiment, the invention provides a crystal comprising a WD repeat domain of an F-box protein. The crystal may also comprise a helical linker of an F-box protein and optionally an F-box domain of an F-box protein. Still further the crystal may comprise a Skp1 protein.

[0017] The present invention also contemplates molecules or molecular complexes that comprise all or parts of either one or more binding pockets of the invention, or homologs of these binding pockets that have similar structure and shape.

[0018] The invention also contemplates a crystal comprising a binding pocket of a SCF E3 ubiquitin ligase involved with substrate recognition and/or orientation in association with a substrate (e.g. CPD motif). A substrate may be complexed or associated with a binding pocket. The invention further contemplates a crystal comprising a binding pocket of a SCF E3 ubiquitin ligase involved with substrate recognition and/or orientation in association with a ligand. A ligand may be a modulator of the activity of a SCF E3 ubiquitin ligase. A ligand may be complexed or associated with a binding pocket

[0019] In an aspect the invention contemplates a crystal comprising a binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation complexed with a substrate from which it is possible to derive structural data for the substrate.

[0020] The shape and structure of a binding pocket may be defined by selected atomic contacts in the pocket. In an embodiment, the binding pocket is defined by one or more atomic interactions or enzyme atomic contacts as set forth in Table 3 or Table 4. Each of the atomic interactions is defined in Table 3 or Table 4 by an atomic contact (more preferably, a specific atom where indicated) on the F-box protein and by an atomic contact (more preferably a specific atom where indicated) on the substrate. The atomic interactions are also defined by an atomic contact on one portion of the F-box protein and an atomic contact on another portion of the F-box protein.

[0021] An isolated polypeptide comprising a binding pocket with the shape and structure of a binding pocket described herein is also within the scope of the invention.

[0022] The invention also provides a method for preparing a crystal of the invention, preferably a crystal of a binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation, or a complex of such a binding pocket and a substrate.

[0023] Crystal structures of the invention enable a model to be produced for a binding pocket of the invention, or complexes or parts thereof. The models will provide structural information about the interactions of a substrate or ligand with a binding pocket. Models may also be produced for substrates and ligands. A model and/or the crystal structure of the present invention may be stored on a computer-readable medium.

[0024] The present invention includes a model of a binding pocket of the present invention that substantially represents the structural coordinates specified in Table 6 or portions thereof. The invention also includes a model that comprises modifications of the structure substantially represented by the structural coordinates specified in Table 6. A model is a representation or image that predicts the actual structure of the binding pocket. As such, a model is a tool that can be used to probe the relationship between a binding pocket's structure and function at the atomic level, and to design molecules that can modulate the binding site and accordingly activity of an F-box protein or SCF complex.

[0025] Thus, the invention provides a model of: (a) a binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation; and (b) a modification of the model of (a).

[0026] A method is also provided for producing a model of the invention representing a binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation, comprising representing amino acids of the binding pocket at substantially the structural coordinates specified in Table 6.

[0027] A crystal and/or model of the invention may be used in a method of determining the secondary and/or tertiary structures of a polypeptide or binding pocket with incompletely characterised structure. Thus, a method is provided for determining at least a portion of the secondary and/or tertiary structure of molecules or molecular complexes which contain at least some structurally similar features to a binding pocket of the invention. This is achieved by using at least some of the structural coordinates set out in Table 6.

[0028] A crystal of the invention may be useful for designing, modeling, identifying, evaluating, and/or synthesizing mimetics of a binding pocket or ligands or substrates that associate with a binding pocket. Such mimetics or ligands may be capable of acting as modulators of an F-box protein or SCF E3 ubiquitin ligase activity, and they may be useful for treating, inhibiting, or preventing diseases modulated by such a protein or ligase.

[0029] Thus, the present invention contemplates a method of identifying a modulator of a F-box protein or an SCF E3 ubiquitin ligase comprising the step of applying the structural coordinates of a binding pocket, or atomic interactions, or atomic contacts of a binding pocket, to computationally evaluate a test ligand or substrate for its ability to associate with the binding pocket, or part thereof. Use of the structural coordinates of a binding pocket, or atomic interactions, or atomic contacts of a binding pocket to design or identify a modulator is also provided.

[0030] In an embodiment, the invention contemplates a method of identifying a modulator of an F-box protein or an SCF E3 ubiquitin ligase comprising determining if a test agent inhibits or potentiates the interaction of an F-box protein or SCF E3 ubiquitin ligase with its substrate.

[0031] The invention further contemplates classes of modulators of F-box proteins or SCF E3 ubiquitin ligases based on the shape and structure of a ligand or substrate defined in relation to the molecule's spatial association with a binding pocket of the invention. Generally, a method is provided for designing potential inhibitors of an F-box protein-substrate interaction or SCF E3 ubiquitin ligase-substrate interaction comprising the step of applying the structural coordinates of a substrate or ligand defined in relation to its spatial association with a binding pocket, or a part thereof, to generate a compound that is capable of associating with the binding pocket.

[0032] It will be appreciated that a modulator of an F-box protein or SCF E3 ubiquitin ligase may be identified by generating an actual secondary or three-dimensional model of a binding pocket, synthesizing a compound, and examining the components to find whether the required interaction occurs.

[0033] A potential modulator of an F-box protein or SCF E3 ubiquitin ligase identified by a method of the present invention may be confirmed as a modulator by synthesizing the compound, and testing its effect on the F-box protein or SCF E3 ubiquitin ligase in an assay.

[0034] A modulator of the invention may be converted using customary methods into pharmaceutical compositions. A modulator may be formulated into a pharmaceutical composition containing a modulator either alone or together with other active substances.

[0035] Therefore, the methods of the invention for identifying modulators may comprise one or more of the following additional steps:

[0036] (a) testing whether the modulator is a modulator of the activity of an F-box protein or an SCF E3 ubiquitin ligase, preferably testing the activity of the modulator in cellular assays and animal model assays;

[0037] (b) modifying the modulator;

[0038] (c) optionally rerunning steps (a) or (b); and

[0039] (d) preparing a pharmaceutical composition comprising the modulator.

[0040] Steps (a), (b) (c) and (d) may be carried out in any order, at different points in time, and they need not be sequential.

[0041] Still another aspect of the present invention provides a method of conducting a drug discovery business comprising:

[0042] (a) providing one or more systems employing the atomic interactions, atomic contacts, or structural coordinates of a binding pocket of an F-box protein or SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation, for identifying agents by their ability to inhibit or potentiate the atomic interactions or atomic contacts of a binding pocket;

[0043] (b) conducting therapeutic profiling of agents identified in step (a), or further analogs thereof, for efficacy and toxicity in animals; and

[0044] (c) formulating a pharmaceutical preparation including one or more agents identified in step (b) as having an acceptable therapeutic profile.

[0045] A further aspect of the present invention provides a method of conducting a drug discovery business comprising:

[0046] (a) providing one or more systems for identifying agents by their ability to inhibit or potentiate the interaction between an F-box protein or SCF complex and its substrate; and

[0047] (b) conducting therapeutic profiling of agents identified in step (a), or further analogs thereof, for efficacy and toxicity in animals; and

[0048] (c) formulating a pharmaceutical preparation including one or more agents identified in step (b) as having an acceptable therapeutic profile.

[0049] In certain embodiments, the subject methods can also include a step of establishing a distribution system for distributing the pharmaceutical preparation for sale, and may optionally include establishing a sales group for marketing the pharmaceutical preparation.

[0050] Yet another aspect of the invention provides a method of conducting a target discovery business comprising:

[0051] (a) providing one or more systems employing the atomic interactions, atomic contacts, or structural coordinates of a binding pocket of an F-box protein or SCF complex involved in substrate recognition and/or orientation, for identifying agents by their ability to inhibit or potentiate the atomic interactions or atomic contacts;

[0052] (b) (optionally) conducting therapeutic profiling of agents identified in step (a) for efficacy and toxicity in animals; and

[0053] (c) licensing, to a third party, the rights for further drug development and/or sales for agents identified in step (a), or analogs thereof.

[0054] Methods are also provided for regulating an F-box protein—substrate interaction or an SCF E3 ubiquitin ligase-substrate interaction by changing a binding pocket involved in substrate recognition and/or orientation. A binding pocket may be changed by altering amino acid residues forming the binding pocket (e.g. introducing mutations) or using a modulator.

[0055] The invention also contemplates a method of treating or preventing a condition or disease associated with an F-box protein or an SCF E3 ubiquitin ligase in a cellular organism, comprising:

[0056] (a) administering a modulator of the invention in an acceptable pharmaceutical preparation; and

[0057] (b) potentiating or inhibiting the F-box protein or SCF E3 ubiquitin ligase to treat or prevent the disease.

[0058] In an embodiment the condition or disease is cancer or Alzheimer's disease.

[0059] The invention provides for the use of a modulator identified by the methods of the invention in the preparation of a medicament to treat or prevent a disease in a cellular organism. Use of modulators of the invention to manufacture a medicament is also provided.

[0060] These and other aspects of the present invention will become evident upon reference to the following detailed description and Tables, and attached drawings.

DESCRIPTION OF THE DRAWINGS AND TABLES

[0061] The present invention will now be described only by way of example, in which reference will be made to the following Figures:

[0062]FIG. 1 shows structure based sequence alignments of (A) Skp1 orthologs and (B) Cdc4 orthologs (red) and paralogs (black). Human Fbw7 and P-TrCP1 are isoforms 1 and 2, respectively. Secondary structure elements are colored as in FIG. 2A. Disordered regions in the crystal structure are shown as dashed lines. Red residues are essential for the Cdc4 function, blue residues strongly influence but do not abrogate function, green residues are non-essential but conserved around the binding pocket, and yellow residues are conserved elsewhere. Circles indicate mutations associated with excessive cell proliferation in flies and/or cancer in humans. Deletion of residues 37-64 in Skp1 is denoted by a triangle and a replacement of two closely placed loops from residues 602-605 and 609-624 is denoted by the underline of the short interloop sequence Gly-Glu-Leu. Insertions to optimize sequence alignments are indicated by number of residues inserted in gray. The non-standard β-strand element 9¹ in ScCdc4 is marked by the red asterisk and is shown in full at the bottom of the alignment. Residues that anchor helix α6 to the F-box domain are marked by green hearts, those that anchor helix α6 to the WD40 domain by red hearts and those that make direct contact between the WD40 domain and F-box domain by blue asterisks. [SEQ ID NOs 3-16.]

[0063]FIG. 2 shows an overview of the Skp1-Cdc4-CPD complex. (A) Ribbon representation of Skp1 and the F-box domain (274-319), the helical linker region (331-366), and the WD40 domain of Cdc4 (367-744) coloured green, red, pink, and blue, respectively. The bound cyclin E derived CPD peptide is shown in purple with the phosphothreonine moiety shown in ball and stick representation. Secondary structure elements are indicated. Positions of disordered loop regions are shown as ribbon breaks. All ribbons representations were generated using Ribbons. (B) Ribbons representation highlighting the WD 40 domain of Cdc4. β propeller blades are denoted PB1 to PB8, and the component secondary structure elements are indicated. Ribbons and CPD peptide are coloured as in (A). Position of the WD40 domain is identical to that in FIGS. 4A to 4C. (C) The structured linkage between the WD40 domain and the F box domain of Cdc4.

[0064]FIG. 3 shows an overview of the CPD binding region of the Ccdc4 WD40 repeat domain. (A) Molecular surface representation of the CPD binding pocket indicating invariant and highly conserved residues. Basic, hydrophobic and small residues are coloured blue, green and orange respectively. The bound CPD is shown in ball and stick representation with carbon, nitrogen, oxygen and phosphorous atoms coloured white, blue, red and yellow respectively. All surface representation were generated using Grasp. (B) Surface representation of CPD binding region as oriented in (A) coloured according to electrostatic potential. Blue and red indicate regions of positive and negative potential respectively (10 to −10 kBT). Residues of the bound CPD are labeled. (C) Stereo ribbons representation highlighting side chains and molecular interactions in the CPD binding pocket. CPD residues and highly conserved and invariant Cdc4 residues are displayed in ball and stick representation. Sites of mutation that give rise to severe loss of function are coloured red, and intermediate loss of function are coloured yellow (see Table 5). All other highly conserved and invariant residues are coloured green. Reference propeller blades of the WD40 repeat domain are indicated. (D) Stereo ribbons representation of the CPD binding pocket highlighting cancer causing mutations in drosophila and human Cdc4 orthologues. Arginine mutations in H-cell lines or entrometrial cells are coloured red. Drosophila mutations are coloured blue and Cdc4 temperature sensitive mutations (Rosamond personal communication) are coloured yellow. (E) Multiple Anomalous Dispersion phased electron density map corresponding to the CPD bound to the WD40 repeat domain of Cdc4. Refined CPD model is shown in ball and stick representation. Figure generate using O. (F) Schematic of CPD binding pocket interactions with the CPD peptide.

[0065]FIG. 4 shows (A) Stereo ribbons representation of the human Skp1-Skp2 complex superimposed on the yeast Skp1-Cdc4-CPD complex. Human Skp1-Skp2 and yeast Skp1-Cdc4 were superimposed through a least squares optimization of Skp1, strands 1 to 3 and a-helices 1 to 6 (RMSD=0.74 Å). The yeast Skp1-Cdc4 complex is coloured as in FIG. 2. Human Skp1, the Skp2 F-box, and the Skp2 Leucine-rich repeat domain are coloured orange, green, and light blue, respectively. Skp1 and F box secondary structure elements that deviate significantly in size and position between the two structures are labeled. (B) Model of the SCFCdc4-CPD E2 complex. The yeast Skp1-Cdc4-CPD complex is coloured as in FIG. 2. Cull, Rbx1, and E2 proteins are coloured pink, red, and light blue, respectively. The arrow indicates the distance between the peptide binding site and the active site cysteine of the E2. The structure was generated using the ternary complex of the cullin cdc53, rbx1, Skp1, previously reported, and superimposing the E2 structure from the E2/Cb1 ring finger structure and the structure of Skp1, Cdc4 and a phosphorylated CPD peptide

[0066]FIG. 5 shows (A) Selection of Sic1 phosphoisoforms by wild type and mutant forms of Cdc4. (B) In vitro ubiquitination of Sic1 isoforms by wild type and mutant SCFCdc4 complexes. (C) Natural CPD sites deviate from the optimal CPD by one or more or more residues.

[0067]FIG. 6 shows substrate orientation within the Skp1-Cdc4-CPD complex. (A) Comparison of the ScSkp1-ScCdc4-CPD complex and the hSkp1-hSkp2 complex. Complexes were superimposed through a least squares optimization of Skp1 β-strands 1 to 3 and a-helices 1 to 6 (RMSD Cα=0.74 Å). Skp1 and F-box secondary structure elements that deviate significantly in size and position between the two structures are labeled. (B) Model of the ubiquitin-E2-SCF^(Cd4)-CPD complex. The arrow indicates the 59 Å distance separating the phosphate group of the CPD and the active site cysteine of the E2.

[0068]FIG. 7 shows the CPD binding pocket of the WD40 domain. (A) Surface representation of the CPD binding pocket indicating invariant and highly conserved residues. Basic (blue), hydrophobic (green) and small polar residues (orange) are shown. The bound CPD is in ball and stick representation with carbon (white), nitrogen (blue), oxygen (red) and phosphorous (yellow) atoms shown. (B) Surface representation of CPD binding region indicating electrostatic potential. Blue and red indicate regions of positive and negative potential, respectively, over the range 10 to −10 kBT. (C) Stereo ribbons representation of side chains and molecular interactions in the CPD binding pocket. Highly conserved and invariant side chains of Cdc4 and the CPD are displayed in ball and stick representation. Sites of mutation that give rise to severe and intermediate loss of function (see FIG. 8) are colored red and blue, respectively; non-essential residues are colored green.

[0069] (D) Schematic of CPD Binding Pocket Interactions With the CPD Peptide.

[0070]FIG. 8 shows structure-guided mutational analysis of Cdc4. (A) Residues required for interaction of phospho-Sic1 and Cdc4 in vitro. Sic1 was phosphorylated with Cln2-Cdc28 kinase and captured onto resin loaded with either wild type or the indicated mutant forms of Skp1-Cdc4 complex. (B) Residues essential for Cdc4 function in vivo. Complementation of a cdc4Δ strain by the indicated alleles was assessed in a plasmid shuffle assay. The R485A, R467A and R534A mutations in Cdc4 have been previously shown to disrupt function in vivo (Nash et al., 2001) and so are not shown. (C) Effect of Cdc4 mutations on sensitivity to increased SIC1 dosage. Strains bearing indicated CDC4 alleles were tested for sensitivity to overexpression of wild type SIC1 and a partially stabilized version, SIC1^(Thr33Val) from the GAL1 promoter. Strains were incubated on galactose or glucose medium for 2 days at 30° C.

[0071]FIG. 9 shows the modulation of the multisite requirement for phospho-Sic1-Cdc4 interaction. (A) All natural CPD sites in Sic1 deviate from the CPD consensus. Underlined residues indicate sub-optimal residues at the P−1 and P−2 positions, boxed residues indicate sub-optimal basic residues at the P+2 to P+5 positions and asterisks indicate a sub-optimal pSer at the P0 position. (B) Capture of Sic1 phospho-isoforms by wild type and mutant Cdc4. Pools of differentially phosphorylated Sic1 were captured on Skp1-Cdc4 resin, using either wild type or the indicated mutant forms of Cdc4 compromised for selection at the P−1 position (V384N W717N) or the P+2 to P+5 positions (K402A R443D). The input and bound phospho-Sic1 isoform pools were resolved by denaturing IEF-2D gel electrophoresis and visualized by anti-Sic1 immunoblot. (C) Ubiquitination of phospho-Sic1 isoforms by wild type and mutant SCF^(Cdc4) complexes. Pools of differently phosphorylated Sic1 were incubated in solution with an equimolar amount of the indicated SCFCdC4 complexes, Cdc34, ubiquitin and ATP for 1 h at 30° C. Input and reaction products were separated and visualized as in (B). Arrows indicate the less phosphorylated forms of Sic1 captured by Cdc4 selection mutants. Asterisk indicates more extensively ubiquitinated species (D) Possible interaction mechanisms for single site and multi-site dependent substrate binding to Cdc4. In a two-site cooperative interaction model (left), a primary high affinity CPD binding site acts in conjunction with a secondary weak CPD binding site. The free energy for the two interactions is additive and so the overall K_(d) increases multiplicatively. In a single-site allovalent interaction (right), multiple low affinity CPD sites engage a single CPD binding site on Cdc4 in equilibrium. The high local concentration of CPD sites increases the probability of binding such that Sic1 is unable to diffuse away from Cdc4 before re-binding occurs. The probability of re-binding increases as an exponential function of the number of CPD sites, thus accounting for the apparent cooperativity of the interaction.

[0072] The present invention will now be described only by way of example, in which reference will be made to the following Tables:

[0073] Table 1 shows data collection, structure determination and refinement statistics of a crystal of the invention.

[0074] Table 2 shows data collection, structure determination and refinement statistics of a crystal of the invention.

[0075] Table 3 shows intermolecular contacts in a binding pocket of the invention.

[0076] Table 4 shows intermolecular contacts in a binding pocket of the invention.

[0077] Table 5 shows mutant cdc4 polyppeptides of the invention. Mutational analysis of the CPD binding surface. Mutants were tested in vitro by ability to bind phosphorylated Sic1 and then captured onto GST-Skp1/Cdc4 resin and detected with anti-sic1 antibody. Mutants were tested in vivo by ability to degrade GAL1-SIC1 or various phosphorylation mutants. Sites are as follows: 3=Thr 33, Thr 45, Ser 76; 4=Thr 5, Thr 33, Thr 45, Ser 76; 5=Thr 2, Thr 5, Thr 33, Thr 45, Ser 76; 6=Thr 2, Thr 5, Thr 33, Thr 45, Ser 69, Ser 76; 7=Thr 2, Thr 5, Thr 33, Thr 45, Ser 69, Ser 76, Ser 80. GAL1-SIC1 plasmids were transformed into a cdc4Δ strain containing a copy of CDC4 on a TRP1 ARS CEN plasmid. Strains were incubated for 2 days at 30° C.

[0078] Table 6 shows the structural coordinates of a binding pocket of the invention.

[0079] In Table 6, from the left, the second column identifies the atom number; the third identifies the atom type; the fourth identifies the amino acid type; the sixth identifies the residue number; the seventh identifies the x coordinates; the eighth identifies the y coordinates; the ninth identifies the z coordinates; the tenth identifies the occupancy; and the eleventh identifies the temperature factor.

[0080] Table 7 lists the oligonucleotides used in the studies described in the examples.

[0081] Table 8 lists the plasmids used in the studies described in the examples.

DETAILED DESCRIPTION OF THE INVENTION

[0082] In accordance with the present invention there may be employed conventional molecular biology, microbiology, and recombinant DNA techniques within the skill of the art. Such techniques are explained fully in the literature. See for example, Sambrook, Fritsch, & Maniatis, Molecular Cloning: A Laboratory Manual, Second Edition (1989) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.); DNA Cloning: A Practical Approach, Volumes I and II (D. N. Glover ed. 1985); Oligonucleotide Synthesis (M. J. Gait ed. 1984); Nucleic Acid Hybridization B. D. Hames & S. J. Higgins eds. (1985); Transcription and Translation B. D. Hames & S. J. Higgins eds (1984); Animal Cell Culture R. I. Freshney, ed. (1986); Immobilized Cells and enzymes IRL Press, (1986); and B. Perbal, A Practical Guide to Molecular Cloning (1984).

[0083] Glossary

[0084] Abbreviations for amino acid residues are the standard 3-letter and/or 1-letter codes used in the art to refer to one of the 20 common L-amino acids. Likewise abbreviations for nucleic acids are the standard codes used in the art.

[0085] “Skp1-Cdc53/Cullin-F-box protein (SCF) E3 ubiquitin ligases” or “SCF complex” refers to a protein complex comprising the adaptor protein Skp1, the scaffold protein cdc53/cullin, a RING-H2 domain protein Rbx1 (also called Roc1 or Hrt1), and an F-box protein, which protein complex augments or otherwise facilitates the ubiquitination of a protein. In certain aspects of the present invention an SCF complex refers to a complex comprising Skp1 and an F box protein or parts thereof.

[0086] In the context of the present invention the term “F-box protein” refers to a protein comprising a characteristic structural motif called the F-box as described in Bai et al, (1996 Cell 86: 263-274) and a protein-protein interaction domain, in particular a WD40 repeat motif or domain. Examples of F-box Proteins include Cdc4 polypeptides, and homologs or portions thereof, preferably portions that interact with a CPD motif (e.g. WD repeat).

[0087] A “WD40 repeat”, “WD40 motif”, or “WD repeat domain” is generally defined as a contiguous sequence of about 25 to 50 amino acids with relatively-well conserved sets of amino acids [i.e. Trp-Asp (WD)] at the ends (amino- and carboxyl-terminal) of the sequence. (For reviews see Neer E J, Schmidt C J, Nambudripad R & Smith TF: “The ancient regulatory-protein family of WD-repeat proteins,” Nature 371, 297-300 (1994) PMID: 8090199; and Smith TF, Gaitatzes CG, Saxena K & Neer EJ: “The WD-repeat: a common architecture for diverse functions,” TIBS 24, 181-185 (1999) PMID: 10322433.) A WD repeat motif or domain can also be defined as a domain of an F-box protein that interacts with a CPD motif or like motif.

[0088] Examples of WD-repeat-containing proteins are cdc4 polypeptides, Met30 homologues and orthologues (see for example, GenBank Accession No. P39014 or MT30_YEAST—SEQ ID NO.17) and β-TRCP homologues and orthologues (see for example, GenBank Accession No. NP_(—)033901—SEQ ID NO.18). Other WD40 repeat-containing proteins will, however, be appreciated by those skilled in the art. A WD40-repeat protein also includes a part of the protein. A person skilled in the art may conduct searches to identify proteins that contain WD-40 repeats, in particular F-box proteins. For example, on-line databases such as GenBank or SwissProt can be searched, either with an entire sequence of a WD-40-containing protein, or with a consensus WD-40 repeat sequence. Various search algorithms and/or programs may be used, including FASTA, BLAST or ENTREZ. FASTA and BLAST are available as a part of the GCG sequence analysis package (University of Wisconsin, Madison, Wis.). ENTREZ is available through the National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Md. The number of WD-40 repeats in a particular protein can range from two to more than eight.

[0089] A “Cdc4 Phospho-Degron motif” or “CPD motif” is a motif that targets substrates for ubiquitination by SCF complexes. The motif can be defined by the consensus sequence X²-X³-pThr-Pro-X⁴ (SEQ ID NO.19), more particularly X²-X³-pThr-Pro-X⁴-X⁵-X⁶-X⁷ (SEQ ID NO.20), wherein X² represents Leu, Pro, or Ile, preferably Leu or Ile; X³ represents Leu, Ile, Val, or Pro, preferably Ile, Leu, or Pro; X⁴ represents any amino acid except basic and bulky hydrophobic amino acids, preferably X⁴, X⁵ and X⁶ represent any amino acid except basic and bulky hydrophobic amino acids, preferably X⁴ is any amino acid except Arg, Lys, Tyr, or Trp, more preferably X⁴ is Ile, Val, Pro, or Gln, preferably X⁵ and X⁶ are any amino acid except Arg, Lys, or Tyr and more preferably X⁵ is Gln, Leu, Met, Thr, or Glu, and X⁶ is Gin, Ala, Thr, Glu, or Ser; and X⁷ is any amino acid, preferably not a basic or bulky hydrophobic amino acid, more preferably X⁷ is any amino acid except Arg, Lys, or Tyr, most preferably X⁷ is Leu, Trp, Asp, Pro, or Gly. A CPD motif preferably comprises the consensus sequence -Leu/Gly/Tyr-Pro-pThr-Pro- (SEQ ID NO.21).

[0090] A CPD motif containing protein includes proteins comprising the CPD motif including but not limited to Gcn4, Cyclin E, Far1, Ash1, Sic1, Pc17, Cdc16, p27^(kip1), Cln2, and transcription factors such as β catenin or IKβα, and homologues of these proteins. The term includes but is not limited to all homologs, orthologs, naturally occurring allelic variants, isoforms and precursors of the polypeptides. Other proteins containing CPD motif sequences may be identified with a protein homology search, for example by searching available databases such as GenBank or SwissProt and various search algorithms and/or programs may be used including FASTA, BLAST (available as a part of the GCG sequence analysis package, University of Wisconsin, Madison, Wis.), or ENTREZ (National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Md.).

[0091] The term “substrate” refers to a protein that interacts with an F-box protein targeting it for ubiquitin-dependent proteolysis, or a protein targeted for F-box dependent degradation. Examples of substrates are CPD motif containing proteins including Gcn4, CyclinE, Far1, Ash1, Sic1, Pc17, Cdc16, p27^(kip1); Cln2, and, transcription factors such as β catenin or Iκβα. The term also refers to a part of a protein that interacts with an F-box protein, including a CPD motif, and analogues of substrates or parts thereof

[0092] A “ligand” refers to a compound or entity that associates with a binding pocket, or modulators of an F-box protein or SCF E3 ubiquitin ligase, including inhibitors. A ligand may be designed rationally by using a model according to the present invention.

[0093] The terms “cdc4 polypeptide” is used to refer to polypeptides of the cdc4 family of proteins characterized by an F-box motif and WD repeats. The term includes but is not limited to all homologs, orthologs, naturally occurring allelic variants, isoforms and precursors of the polypeptides of GenBank Accession Nos. S56245 or SEQ ID NO. 22 (Saccharomyces cerevisiae cdc4), CAA65538 or SEQ ID NO. 23 (Candida albicans cdc4), AAL07271 or SEQ ID NO.24 (human cdc4), AAC47809 or SEQ ID NO.25 (sel-10), AAK57547 or SEQ ID NO.26 (Homo sapiens F-box protein FBW7), and AAG09623F or SEQ ID NO. 27 (Homo sapiens F box protein FBX30). In general, for example, naturally occurring allelic variants will share significant homology (70-90%) to these sequences. Allelic variants may contain conservative amino acid substitutions from cdc4 sequences or will contain a substitution of an amino acid from a corresponding position in a cdc4 homologue such as, for example, the human homologue. [See Strohmaier,H., Nature 413 (6853), 316-322 (2001) for a description and sequence of human cdc4]. The term also includes the mutant cdc4 polypeptides described herein. FIG. 1 shows a structure based sequence alignment of cdc4 orthologs and paralogs.

[0094] The term “cdc53” or “cdc53 polypeptide” is used interchangeably herein with the term “cullins” when referring to a vertebrate homolog of the yeast cdc53 protein. The term “cullin polypeptide” or “cullin protein”, refers to a member of the cullins family, e.g., any one of cul-1, -2, -3, -4, -5, or -6. The term includes but is not limited to all homologs, naturally occurring allelic variants, isoforms and precursors of a cdc53 polypeptide or cullin of GenBank Accession Nos. AAB38821 or SEQ ID NO. 28 (Saccharomyces cerevisiae cdc53), AAC36304 or SEQ ID NO. 29 (Homo sapiens cullin 3), AAC51190 or SEQ ID NO. 30 (Homo sapiens cullin 2), NP 003581 or SEQ ID NO. 31 (Homo sapiens cullin 3), AF126404_(—)1 or SEQ ID NO. 32 (Homo sapiens cullin 2), CUL1_CAEEL or SEQ ID NO. 33 (Caenorhabditis elegans cullin 1), AAA85085 or SEQ ID NO. 34 (Drosophila melanogaster cullin 1) and the cullins described in Kipreos ET (Cell 1996 Jun. 14;85(6):829-39). In general for example, naturally occurring allelic variants of cdc53 will share significant homology (70-90%) to the cdc53 or cullin sequences. Allelic variants may contain conservative amino acid substitutions from the cdc4 sequence or will contain a substitution of an amino acid from a corresponding position in a cdc4 homolog such as, for example, the human homolog.

[0095] The term “Skp1” or “Skp1 polypeptide” is used to refer to polypeptides that connect cell cycle regulators to the ubiquitin proteolysis machinery by associating with F-box proteins through the F-box motif. The term includes but is not limited to all homologs, naturally occurring allelic variants, isoforms and precursors of Skp1 of GenBank Accession Nos. SKP1_SCHPO or SEQ ID NO. 35 (Schizosaccharomyces pombe), BAB62325 or SEQ ID NO. 36 (Schizosaccharomyces pombe), AAC49492 or SEQ ID NO. 37 (Saccharomyces cerevisiae), and AAB17500 or SEQ ID NO. 38 (Saccharomyces cerevisiae). In general, for example, naturally occurring allelic variants of Skp1 will share significant homology (70-90%) to the Skp1 sequences. Allelic variants may contain conservative amino acid substitutions from the Skp1 sequence or will contain a substitution of an amino acid from a corresponding position in a Skp1 homolog such as, for example, the human homolog. FIG. 1 shows a structure based sequence alignment of Skp1 homologues.

[0096] A CPD motif and WD repeat or proteins containing same, cdc4 polypeptides, cdc53, Skp1, substrates, and SCF complexes, may be from any species, particularly a mammalian species, including bovine, ovine, porcine, murine, equine, preferably the human species, and from any source, whether natural, synthetic, semi-synthetic, or recombinant.

[0097] The term “agonist” of a binding pocket refers to a compound or ligand that interacts with the binding pocket and maintains or increases the activity of the binding pocket to which it binds. The term includes partial agonists and inverse agonists. Agonists may include proteins, peptides, nucleic acids, carbohydrates, or any other molecules that bind to a binding pocket. Agonists also include a molecule derived from a binding pocket. Peptide mimetics, synthetic molecules with physical structures designed to mimic structural features of particular peptides, may serve as agonists. The stimulation may be direct, or indirect, or by a competitive or non-competitive mechanism. The term includes partial agonists and inverse agonists.

[0098] As used herein, the term “partial agonist” means an agonist that is unable to evoke the maximal response of a biological system, even at a concentration sufficient to saturate the specific receptors.

[0099] As used herein, the term “partial inverse agonist” is an inverse agonist that evokes a submaximal response to a biological system, even at a concentration sufficient to saturate the specific receptors. At high concentrations, it will diminish the actions of a full inverse agonist.

[0100] The term “antagonist”, as used herein, refers to a ligand or compound that binds a binding pocket but does not maintain the activity of the binding pocket to which it binds. The term can also includes a ligand that reduces the action of another agent, such as an agonist. An antagonistic action may result from a combination of the substance being antagonised (chemical antagonism) or the production of an opposite effect through a different protein (functional antagonism or physiological antagonism) or as a consequence of competition for the binding site of an intermediate that links a protein to the effect observed (indirect antagonism). The antagonist may act at the same site as the agonist (competitive antagonism). Antagonists may include proteins, peptides, nucleic acids, carbohydrates, or any other molecules that bind to a binding pocket. Antagonists also include a molecule derived from a binding pocket. Peptide mimetics, synthetic molecules with physical structures designed to mimic structural features of particular peptides, may serve

[0101] As used herein, the term “competitive antagonism” refers to the competition between an agonist and an antagonist for a binding pocket of a protein that occurs when the binding of agonist and antagonist becomes mutually exclusive. This may be because the agonist and antagonist compete for the same binding sites or pockets, or combine with adjacent but overlapping sites. A third possibility is that different sites are involved but that they influence the receptor macromolecules in such a way that agonist and antagonist molecules cannot be bound at the same time. If the agonist and antagonist form only short lived combinations with a binding pocket so that equilibrium between agonist, antagonist and binding pocket is reached during the presence of the agonist, the antagonism will be surmountable over a wide range of concentrations. In contrast, some antagonists, when in close enough proximity to their binding site, may form a stable covalent bond with it and the antagonism becomes insurmountable when no spare receptors remain.

[0102] By being “derived from” a binding pocket is meant any molecular entity which is identical or substantially equivalent to the binding pocket. A peptide derived from a binding pocket may encompass the amino acid sequence of a naturally occurring binding pocket, any portion of that binding pocket or other molecular entity that functions to bind to an associated or interacting binding pocket. A peptide derived from such a binding pocket will interact directly or indirectly with an associated molecule in such a way as to mimic the native binding pocket. Such peptides may include competitive inhibitors, peptide mimetics, and the like. The entity will not include a full length sequence of a wild-type molecule. Peptide mimetics, synthetic molecules with physical structures designed to mimic structural features of particular peptides, may serve as inhibitors or enhancers.

[0103] “Peptide mimetics” are structures which serve as substitutes for peptides in interactions between molecules (See Morgan et al (1989), Ann. Reports Med. Chem. 24:243-252 for a review). Peptide mimetics include synthetic structures which may or may not contain amino acids and/or peptide bonds but retain the structural and functional features of a peptide, or agonist or antagonist (i.e. enhancer or inhibitor) of a binding pocket. Peptide mimetics also include peptoids, oligopeptoids (Simon et al (1972) Proc. Natl. Acad, Sci USA 89:9367); and peptide libraries containing peptides of a designed length representing all possible sequences of amino acids corresponding to a motif, peptide, or agonist or antagonist (i.e. enhancer or inhibitor) of the invention.

[0104] Sequences are “homologous” or considered “homologs” when at least about 70% (preferably at least about 80 to 90%, and most preferably at least 95%) of the nucleotides or amino acids match over a defined length of the molecule. “Substantially homologous” also includes sequences showing identity to the specified sequence. Percent identity can be determined electronically, e.g., by using the MEGALIGN program (DNASTAR, Inc., Madison Wis.) which can create alignments between two or more sequences according to different methods, e.g., the clustal method. (See, e.g., Higgins, D. G. and P. M. Sharp (1988) Gene 73:237-244.) Percent identity can also be determined by other methods known in the art, (e.g., the Jotun Hein method. (See, e.g., Hein, J. (1990) Methods Enzymol. 183:626-645) or by varying hybridization conditions). Preferably, the amino acid or nucleic acid sequences have an alignment score of greater than 5 (in standard deviation units) using the program ALIGN with the mutation gap matrix and a gap penalty of 6 or greater (Dayhoff).

[0105] Binding Pocket

[0106] “Binding pocket” refers to a region or site of an F-box protein or molecular complex thereof (e.g. Skp1-F-box complex, SCF E3 ubiquitin ligase) involved in substrate selection and/or orientation. As the result of its shape, a binding pocket associates with another region of an F-box protein or SCF complex or with a substrate or a part thereof.

[0107] In an aspect of the invention a binding pocket comprises one or more of the residues involved in selection and/or orientation of a substrate or ligand.

[0108] In an aspect of the invention a binding pocket is provided that comprises the WD40 repeat domain of an F-box protein. In another embodiment the binding pocket comprises a WD40 repeat domain and a helical linker of an F-box protein. In a further embodiment, the binding pocket comprises a WD40 repeat domain, a helical linker and an F-box domain of an F-box protein. In an embodiment the F-box protein is a cdc4 polypeptide or portion thereof.

[0109] A binding pocket of the invention may comprise a WD40 repeat domain characterized by one or more of the following characteristics:

[0110] (a) a 7 or 8 blade β-propeller structure, in particular a 8 blade β-propeller structure;

[0111] (b) a disk like structure characterized by a cavity in the middle and two opposing circular surfaces of different size;

[0112] (c) a conical frustum of about 40 Å top surface and about 50 Å bottom surface, an overall thickness of 30 Å and a central pore of 6 Å diameter; and

[0113] (d) a CPD binding site on the top surface of the frustum of (c) and running across the edge of the pore, while the bottom surface of the frustum links to the F-box domain.

[0114] A binding pocket of the invention may be characterized by one or more of the following characteristics:

[0115] (i) a dedicated pThr-Pro binding pocket;

[0116] (ii) a deep hydrophobic pocket that selects hydrophobic residues N-terminal to the phosphorylation site of a CPD, and

[0117] (iii) a through space electrostatic selection against basic residues C-terminal to the phosphorylation site of a CPD.

[0118] A binding pocket of the invention may comprise a helical linker characterized by a helices that form a stalk and pedestal like structure that connects and orients a WD repeat domain. The helical linker binding pocket can also be characterized by one or more of the following:

[0119] (a) a helix (e.g. α6 in FIG. 2 or FIG. 6) that is 30 Å in length and is anchored at its N-terminus to the hydrophobic core of the F-box/helical extension and at its C-terminus to the hydrophobic core of a WD repeat domain,

[0120] (b) the helix of (a) (e.g. α6) anchored at its amino terminus to an F-box through hydrophobic interactions (e.g. involving α6 residues Phe 355, Leu356, and F box residues Ile295, Ile296, Leu315, Leu 319 and Trp316 of Cdc4 or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0121] (c) a second helix (e.g. helix 5) packed along the base of the helix of (a) or (b) opposite to the F-box domain through hydrophobic interactions (e.g. involving Tyr342, Leu338, and Leu 334 of Cdc4 or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0122] (d) the helix of (a) (e.g. helix α6) anchored at its C-terminus through hydrophobic interactions;

[0123] (e) a C-terminal end of helix α6 inserted obliquely between propeller blades P7 and β8 of a WD40 domain through van der Wals and hydrophobic interactions (e.g. involving Trp365 and Ile361 with WD40 domain residues Val687, Ile696, Leu726, and Phe743 in β-propeller blades 7 and 8 of Cdc4 or the corresponding residues in Cdc4 homologs, variants, precursors etc.).

[0124] A CPD motif binding pocket of the invention may comprise a hydrophobic pocket that surrounds the open central channel of a 7 or 8 blade WD repeat propeller. A binding pocket of Cdc4 is more particularly characterized by one or more of the following:

[0125] (a) a WD repeat domain surface composed of invariant and highly conserved residues from β-propeller blades;

[0126] (b) a three-sided pocket formed by Trp426, Thr386, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0127] (c) a three-sided pocket formed by Trp426, Thr441, Thr 465, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0128] (d) a hydrophobic pocket composed of Trp 426, Trp 717, Thr 386, and Val 384 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0129] (e) a pocket formed by Leu634, Met590, and Tyr574 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.); and

[0130] (f) a pocket formed by Arg485, Arg467, Arg534, Tyr548, and Arg572 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0131] A binding pocket may comprise one or more of the amino acid residues for an F-box protein crystal or F-box protein—substrate crystal identified in Table 3 or Table 4. In an aspect the binding pocket comprises the atomic contacts of atomic interactions 1 to 4 or interactions 5 to 8/9 identified in Table 3 or Table 4. In an aspect of the invention the binding pocket comprises all of the amino acid residues identified in Table 3 or Table 4.

[0132] The term “binding pocket” (BP) also includes a homolog of the binding pocket or a portion thereof. As used herein, the term “homolog” in reference to a binding pocket refers to a binding pocket or a portion thereof which may have deletions, insertions or substitutions of amino acid residues as long as the binding specificity is retained. In this regard, deliberate amino acid substitutions may be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity, and/or the amphipathic nature of the residues as long as the binding specificity of the binding pocket is retained.

[0133] As used herein, the term “portion thereof” means the structural coordinates corresponding to a sufficient number of amino acid residues of a binding pocket (or homologs thereof) that are capable of associating with a substrate (e.g. CPD motif) or ligand. For example, the structural coordinates provided in a crystal structure may contain a subset of the amino acid residues in a binding pocket which may be useful in the modelling and design of compounds that bind to the binding pocket.

[0134] Crystal

[0135] The invention provides crystal structures. As used herein, the term “crystal” or “crystalline” means a structure (such as a three dimensional (3D) solid aggregate) in which the plane faces intersect at definite angles and in which there is a regular structure (such as internal structure) of the constituent chemical species. The term “crystal” can include any one of: a solid physical crystal form such as an experimentally prepared crystal, a crystal structure derivable from the crystal (including secondary and/or tertiary and/or quaternary structural elements), a 2D and/or 3D model based on the crystal structure, a representation thereof such as a schematic representation thereof or a diagrammatic representation thereof, or a data set thereof for a computer.

[0136] In one aspect, the crystal is usable in X-ray crystallography techniques. Here, the crystals used can withstand exposure to X-ray beams used to produce a diffraction pattern data necessary to solve the X-ray crystallographic structure. A crystal may be characterized as being capable of diffracting x-rays in a pattern defined by one of the crystal forms depicted in Blundel et al 1976, Protein Crystallography, Academic Press.

[0137] A crystal of the invention is generally produced in a laboratory; that is, it is an isolated crystal produced by an individual.

[0138] The invention contemplates a crystal comprising a binding pocket of the invention, in particular a binding pocket of an F-box protein or SCF complex or portion thereof, involved in substrate selection and/or orientation.

[0139] In an aspect of the invention a crystal is provided that comprises the WD40 repeat domain of an F-box protein, in particular Cdc4. In another embodiment the crystal comprises a WD40 repeat domain and a helical linker of an F-box protein. In a further embodiment, the crystal comprises a WD40 repeat domain, a helical linker and an F-box domain of an F-box protein. In an embodiment the F-box protein is a cdc4 polypeptide or portion thereof.

[0140] A crystal of the invention comprising a WD40 repeat domain, in particular a Cdc4 polypeptide WD40 repeat domain, may be characterized by one or more of the following characteristics:

[0141] (a) a 7 or 8 blade β-propeller structure, in particular a 8 blade β-propeller structure;

[0142] (b) a disk like structure characterized by a cavity in the middle and two opposing circular surfaces of different size;

[0143] (c) a conical frustum of about 40 Å top surface and about 50 Å bottom surface, an overall thickness of 30 Å and a central pore of 6 Å diameter; and

[0144] (d) a CPD binding site on the top surface of the frustum of (c) and running across the edge of the pore, while the bottom surface of the frustum links to the F-box domain.

[0145] Each blade of the α-propeller structure can be further characterized by 4 anti-parallel α-strands. The disk like structure can also be characterized by a smaller surface comprising a CPD binding site and a bottom surface anchored by a helix (e.g. helix α6) of a helical extension of the F-box protein. As illustrated in FIGS. 2 and 3 the structure is further characterized by β-propeller blade 2 consisting of 5β-strands and a strand β9′ forming a parallel arrangement with strand β9.

[0146] A crystal of a binding pocket of an F-box protein of the invention, in particular a Cdc4 polypeptide, may be characterized by one or more of the following characteristics:

[0147] (i) a dedicated pThr-Pro binding pocket;

[0148] (ii) a deep hydrophobic pocket that selects hydrophobic residues N-terminal to the phosphorylation site of a CPD motif, and

[0149] (iii) a through space electrostatic selection against basic residues C-terminal to the phosphorylation site of a CPD motif.

[0150] In a preferred embodiment, a crystal of a WD40 repeat domain has the structure illustrated in FIG. 2 or 3.

[0151] A crystal of the invention can comprise a helical linker characterized by α helices that form a stalk and pedestal like structure that connects and orients a WD repeat domain. A helical linker structure of a Cdc4 polypeptide can also be characterized by one or more of the following structures: (a) a helix (e.g. α6 in FIG. 2 or FIG. 6) that is

[0152] 30 Å in length and is anchored at its N-terminus to the hydrophobic core of the F-box/helical extension and at its C-terminus to the hydrophobic core of a WD repeat domain,

[0153] (b) the helix of (a) (e.g. α6) anchored at its amino terminus to an F-box through hydrophobic interactions (e.g. involving α6 residues Phe 355, Leu356, and F box residues Ile295, Ile296, Leu315, and Trp316 or the corresponding residues in Cdc4 homologs, variants, precursors etc.));

[0154] (c) a second helix (e.g. helix 5) packed along the base of the helix of (a) or (b) opposite to the F-box domain through hydrophobic interactions (e.g. involving Tyr342, Leu338, and Leu 334) (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0155] (d) the helix of (a) (e.g. helix α6) anchored at its C-terminus through hydrophobic interactions;

[0156] (e) a C-terminal end of helix α6 inserted obliquely between propeller blades β7 and β8 of the WD40 domain through van der Wals and hydrophobic interactions (e.g. involving Trp365 and Ile361 with WD40 domain residues Val687, 11e696, Leu726, and Phe743 in β-propeller bnlades 7 and 8 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.).

[0157] In a preferred embodiment, a crystal of a helical linker has the structure illustrated in FIG. 2.

[0158] A crystal of the invention may comprise a CPD motif binding pocket that is characterized by a hydrophobic pocket that surrounds the open central channel of a 7 or 8 blade WD repeat propeller. A crystal of a Cdc4 polypeptide may be more particularly characterized by one or more of the following:

[0159] (a) a WD repeat domain surface composed of invariant and highly conserved residues from β-propeller blades;

[0160] (b) a three-sided pocket formed by Trp426, Thr386, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0161] (c) a three-sided pocket formed by Trp426, Thr441, Thr 465, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0162] (d) a hydrophobic pocket composed of Trp 426, Trp 717, Thr 386, and Val 384(or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0163] (e) a pocket formed by Leu634, MetS90, and Tyr574 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.); and

[0164] (f) a pocket formed by Arg485, Arg467, Arg534, Tyr548, and Arg572 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.).

[0165] In a preferred embodiment, a crystal of a CPD motif binding pocket has the structure illustrated in FIG. 3, 4, 6 or 7

[0166] In a further aspect of the invention a crystal is provided comprising an F-box domain comprising five a helices. In a preferred embodiment, a crystal of an F-box domain has the structure illustrated in FIG. 2 or FIG. 6.

[0167] A crystal of the invention may comprise an F-box protein characterized by one or more of the following:

[0168] (a) an F-box domain consisting of five a helices;

[0169] (b) a WD 40 repeat domain characterized by 7 or 8 copies of a WD40 repeat motif forming a 7 or 8 blade α-propeller structure; and

[0170] (c) two a helices that together with two a helices of the F-box domain forming a stalk and pedestal like structure that connects and orients the WD40 domain.

[0171] With reference to a crystal of the present invention, residues in a binding pocket may be defined by their spatial proximity to a substrate or ligand in the crystal structure. For example, a binding pocket may be defined by its proximity to a substrate molecule, or modulator.

[0172] A crystal of the invention includes a binding pocket in association with one or more moieties, including heavy-metal atoms i.e. a derivative crystal, or one or more substrates or ligands i.e. a co-crystal.

[0173] The term “associate”, “association” or “associating” refers to a condition of proximity between a moiety (i.e. chemical entity or compound or portions or fragments thereof), and a binding pocket. The association may be non-covalent i.e. where the juxtaposition is energetically favored by for example, hydrogen-bonding, van der Waals, or electrostatic or hydrophobic interactions, or it may be covalent.

[0174] The term “heavy-metal atoms” refers to an atom that can be used to solve an x-ray crystallography phase problem, including but not limited to a transition element, a lanthanide metal, or an actinide metal. Lanthanide metals include elements with atomic numbers between 57 and 71, inclusive. Actinide metals include elements with atomic numbers between 89 and 103, inclusive.

[0175] Multiwavelength anomalous diffraction (MAD) phasing may be used to solve protein structures using selenomethionyl (SeMet) proteins. Therefore, a complex of the invention may comprise a crystalline binding pocket with selenium on the methionine residues of the protein.

[0176] A crystal may comprise a complex between a binding pocket and one or more substrates or ligands. In other words the binding pocket may be associated with one or more ligands or molecules in the crystal. The ligand may be any compound that is capable of stably and specifically associating with the binding pocket. A ligand may, for example, be a modulator or analogue thereof. Therefore, a crystal may comprise a binding pocket comprising two or more of the amino acid residues of an F-box protein structure as described herein, that are capable of associating with or coordinating a CPD motif as described herein.

[0177] In an embodiment, a crystal of the invention comprises a complex between a binding pocket, and a substrate or analogue thereof. Therefore, the present invention also provides a crystal comprising a binding pocket of an F-box protein or a SCF complex and a substrate or analogue thereof. A substrate may be for example, a CPD motif or CPD motif containing protein. An analog of a substrate is one which mimics the substrate molecule, binding in the binding pocket, but which is incapable (or has a significantly reduced capacity) to take part in SCF E3 ubiquitin ligase activity.

[0178] In an embodiment, a crystal comprising a WD repeat domain of a Cdc4 polypeptide and a CPD motif is provided, which is characterized by one or more of the following:

[0179] (a) a WD 40 repeat domain characterized by 7 or 8 copies of a WD40 repeat motif forming a 7 or 8 blade β-propeller structure comprising β-propeller blades 1, 2, 3, 4, 5, 6, and 7, and optionally 8;

[0180] (b) the CPD motif binds in an extended manner across β-propeller blade 2 with the N-terminus oriented toward the central cavity of the WD repeat domain and the C-terminus oriented towards the outer rim;

[0181] (c) the CPD binding surface of the WD repeat domain is composed of invariant and highly conserved residues from β-propeller blades 1 to 6 and optionally 8;

[0182] (d) a P0 phosphate pThr of the CPD motif forms direct electrostatic interactions with the guanidium groups of Arg 485, Arg 467, and Arg 534 and a direct hydrogen bond with the side chain of Tyr 548 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0183] (e) P+1 proline side chains of the CPD motif project into a three-sided pocket on the CPD binding surface formed by the side chain of Trp 426 and Arg485 or Trp 426, Thr441, Thr465, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.); and

[0184] (f) P+1 leucine side chain of the CPD motif is oriented towards a hydrophobic pocket composed of residues Trp 426, Trp 717, Thr 386, and Val 384 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.).

[0185] In a preferred embodiment, a crystal of a complex of a WD repeat domain and a CPD motif has the structure illustrated in FIG. 2, 3, 4, 6, or 7.

[0186] A crystal or secondary or three-dimensional structure of a binding pocket of an F-box protein, may be specifically defined by one or more of the atomic contacts of the atomic interactions identified in Table 3 or Table 4. The atomic interactions in Table 3 or Table 4 are defined therein by an atomic contact (more preferably, a specific atom of an amino acid residue where indicated) on the F box protein, in particular on the WD40 repeat domain or helical linker, and an atomic contact (more preferably, a specific atom of an amino acid residue where indicated) on a substrate e.g. CPD motif, or an atomic contact (more preferably, a specific atom of an amino acid residue where indicated) on another region of the F-box protein (e.g. helical linker or F-box domain). In certain embodiments, a crystal of the invention comprises the atomic contacts of atomic interactions 1 to 8 identified in Table 3 or Table 4. In certain particular embodiments a crystal is provided comprising the atomic contacts of atomic interactions 1 to −4 or 5 to 8. Preferably, a crystal is defined by the atoms of the atomic contacts in the binding pocket having the structural coordinates for the atoms listed in Table 6.

[0187] A structure of a complex may be defined by selected intermolecular contacts, preferably the structural coordinates of the intermolecular contacts as defined in Table 6, preferably interactions 5 to 8.

[0188] A crystal of the invention may comprise one or more of the following groups of amino acid residues: (a) Ile 295, Ile 296, Leu 315, Trp 316, Leu 319, Phe 355, and Leu 356; (b) Val 687, Ile 696, Leu 726, Phe 743, Trp 365, and Ile 364; (c) Asn 684, Arg 700, and Glu 323; (d) Arg 485, Arg 467, Arg 534, Tyr 548; (e) Trp 426, Arg 485, Thr 441, and Thr 465; (f) Trp 426, Trp 717, Thr 386, and Val 384; (g) Tyr 574, Thr 386 and Val 384; (h) Tyr 574, Met 590, and Leo 634; and (i) the corresponding residues in Cdc4 homologs, paralogs, variants, or precursors. Preferably the atoms of the amino acid residues have the structural coordinates as set out in Table 6.

[0189] A crystal of the invention may enable the determination of structural data for a substrate or ligand. In order to be able to derive structural data for a ligand, or substrate it is necessary for the molecule to have sufficiently strong electron density to enable a model of the molecule to be built using standard techniques. For example, there should be sufficient electron density to allow a model to be built using XTALVIEW (McRee 1992 J. Mol. Graphics. 10 44-46).

[0190] A crystal of the invention may belong to space group P3₂. The term “space group” refers to the lattice and symmetry of the crystal. In a space group designation the capital letter indicates the lattice type and the other symbols represent symmetry operations that can be carried out on the contents of the asymmetric unit without changing its appearance.

[0191] A crystal of the invention may comprise a unit cell having the following unit dimensions: α=107.7 Å, b=107.7 Å, c=168.3 Å, α=γ=90°, p=120°. The term “unit cell” refers to the smallest and simplest volume element (i.e. parallelpiped-shaped block) of a crystal that is completely representative of the unit of pattern of the crystal. The unit cell axial lengths are represented by a, b, and c. Those of skill in the art understand that a set of atomic coordinates determined by X-ray crystallography is not without standard error.

[0192] In a preferred embodiment, a crystal of the invention has the structural coordinates as shown in Table 6. As used herein, the term “structural coordinates” refers to a set of values that define the position of one or more amino acid residues with reference to a system of axes. The term refers to a data set that defines the three dimensional structure of a molecule or molecules (e.g. Cartesian coordinates, temperature factors, and occupancies). Structural coordinates can be slightly modified and still render nearly identical three dimensional structures. A measure of a unique set of structural coordinates is the root-mean-square deviation of the resulting structure. Structural coordinates that render three dimensional structures (in particular a three dimensional structure of a ligand binding pocket) that deviate from one another by a root-mean-square deviation of less than 5 Å, 4 Å, 3 Å, 2 Å, 1.5 Å, 1.0 Å, or 0.5 Å may be viewed by a person of ordinary skill in the art as very similar.

[0193] Variations in structural coordinates may be generated because of mathematical manipulations of the structural coordinates of a structure or binding pocket described herein. For example, the structural coordinates of Table 6 may be manipulated by crystallographic permutations of the structural coordinates, fractionalization of the structural coordinates, integer additions or substractions to sets of the structural coordinates, inversion of the structural coordinates or any combination of the above.

[0194] Variations in the crystal structure due to mutations, additions, substitutions, and/or deletions of the amino acids, or other changes in any of the components that make up the crystal may also account for modifications in structural coordinates. If such modifications are within an acceptable standard error as compared to the original structural coordinates, the resulting structure may be the same. Therefore, a ligand that bound to a binding pocket of an F-box protein, would also be expected to bind to another binding pocket whose structural coordinates defined a shape that fell within the acceptable error. Such modified structures of a binding pocket thereof are also within the scope of the invention.

[0195] Various computational analyses may be used to determine whether a molecule or the binding pocket thereof is sufficiently similar to all or parts of an F-box or a binding pocket thereof. Such analyses may be carried out using conventional software applications and methods as described herein.

[0196] A crystal of the invention may also be specifically characterised by the parameters, diffraction statistics and/or refinement statistics set out in Table 1 or in Table 2.

[0197] Illustrations of particular crystals of the invention are shown in FIGS. 2, 3, 4, 6 and 7.

[0198] Method of Making a Crystal

[0199] The present invention also provides a method of making a crystal according to the invention. The crystal may be formed from an aqueous solution comprising a purified polypeptide comprising an F-box protein including a variant, part, homolog, or fragment thereof (e.g. a binding pocket). A method may utilize a purified polypeptide comprising a binding pocket to form a crystal. A method may utilize one or more purified mutant polypeptides as described herein. In an embodiment, a mutant cdc4 polypeptide is used to make crystals.

[0200] The term “purified” in reference to a polypeptide, does not require absolute purity such as a homogenous preparation rather it represents an indication that the polypeptide is relatively purer than in the natural environment. Generally, a purified polypeptide is substantially free of other proteins, lipids, carbohydrates, or other materials with which it is naturally associated, preferably at a functionally significant level for example at least 85% pure, more preferably at least 95% pure, most preferably at least 99% pure. A skilled artisan can purify a polypeptide comprising using standard techniques for protein purification. A substantially pure polypeptide will yield a single major band on a non-reducing polyacrylamide gel. Purity of the polypeptide can also be determined by amino-terminal amino acid sequence analysis.

[0201] A polypeptide used in the method may be chemically synthesized in whole or in part using techniques that are well-known in the art. Alternatively, methods are well known to the skilled artisan to construct expression vectors containing a native or mutated protein coding sequence and appropriate transcriptional/translational control signals. These methods include in vitro recombinant DNA techniques, synthetic techniques, and in vivo recombination/genetic recombination. See for example the techniques described in Sambrook et al. (Molecular Cloning: A Laboratory Manual, 2nd Edition, Cold Spring Harbor Laboratory press (1989)), and other laboratory textbooks. (See also Sarker et al, Glycoconjugate J. 7:380, 1990; Sarker et al, Proc. Natl. Acad, Sci. USA 88:234-238, 1991, Sarker et al, Glycoconjugate J. 11: 204-209, 1994; Hull et al, Biochem Biophys Res Commun 176:608, 1991 and Pownall et al, Genomics 12:699-704, 1992).

[0202] Crystals may be grown from an aqueous solution containing the purified polypeptide by a variety of conventional processes. These processes include batch, liquid, bridge, dialysis, vapor diffusion, and hanging drop methods. (See for example, McPherson, 1982 John Wiley, New York; McPherson, 1990, Eur. J. Biochem. 189: 1-23; Webber. 1991, Adv. Protein Chem. 41:1-36). Generally, native crystals of the invention are grown by adding precipitants to the concentrated solution of the polypeptide. The precipitants are added at a concentration just below that necessary to precipitate the protein. Water is removed by controlled evaporation to produce precipitating conditions, which are maintained until crystal growth ceases.

[0203] Derivative crystals of the invention can be obtained by soaking native crystals in a solution containing salts of heavy metal atoms. A complex of the invention can be obtained by soaking a native crystal in a solution containing a compound that binds the polypeptide, or they can be obtained by co-crystallizing the polypeptide in the presence of one or more compounds. In order to obtain co-crystals with a compound which binds deep within the tertiary structure of the polypeptide it is necessary to use the second method.

[0204] Once the crystal is grown it can be placed in a glass capillary tube and mounted onto a holding device connected to an X-ray generator and an X-ray detection device. Collection of X-ray diffraction patterns are well documented by those skilled in the art (See for example, Ducruix and Geige, 1992, IRL Press, Oxford, England). A beam of X-rays enter the crystal and diffract from the crystal. An X-ray detection device can be utilized to record the diffraction patterns emanating from the crystal. Suitable devices include the Marr 345 imaging plate detector system with an RU200 rotating anode generator.

[0205] Multiwavelength anomalous diffraction (MAD) phasing using selenomethionyl (SeMet) proteins may be used to determine a crystal of the invention. Thus, the invention contemplates a method for determining a crystal structure of the invention using a selenomethionyl derivative of an F-box protein or SCF complex, including a variant, part, homolog or fragement thereof.

[0206] Methods for obtaining the three dimensional structure of the crystalline form of a molecule or complex are described herein and known to those skilled in the art (see Ducruix and Geige 1992, IRL Press, Oxford, England). Generally, the x-ray crystal structure is given by the diffraction patterns. Each diffraction pattern reflection is characterized as a vector and the data collected at this stage determines the amplitude of each vector. The phases of the vectors may be determined by the isomorphous replacement method where heavy atoms soaked into the crystal are used as reference points in the X-ray analysis (see for example, Otwinowski, 1991, Daresbury, United Kingdom, 80-86). The phases of the vectors may also be determined by molecular replacement (see for example, Naraza, 1994, Proteins 11:281-296). The amplitudes and phases of vectors from the crystalline form determined in accordance with these methods can be used to analyze other related crystalline polypeptides.

[0207] The unit cell dimensions and symmetry, and vector amplitude and phase information can be used in a Fourier transform function to calculate the electron density in the unit cell i.e. to generate an experimental electron density map. This may be accomplished using the PHASES package (Furey, 1990). Amino acid sequence structures are fit to the experimental electron density map (i.e. model building) using computer programs (e.g. Jones, TA. et al, Acta Crystallogr A47, 100-119, 1991). This structure can also be used to calculate a theoretical electron density map. The theoretical and experimental electron density maps can be compared and the agreement between the maps can be described by a parameter referred to as R-factor. A high degree of overlap in the maps is represented by a low value R-factor. The R-factor can be minimized by using computer programs that refine the structure to achieve agreement between the theoretical and observed electron density map. For example, the XPLOR program, developed by Brunger (1992, Nature 355:472-475) can be used for model refinement.

[0208] A three dimensional structure of the molecule or complex may be described by atoms that fit the theoretical electron density characterized by a minimum R value. Files can be created for the structure that defines each atom by coordinates in three dimensions.

[0209] Mutant CDC4 Polypeptides

[0210] The present invention provides novel mutant cdc4 polypeptides.

[0211] A particular mutant of the present invention is a polypeptide having an amino acid sequence of a cdc4 polypeptide wherein amino acid residues are replaced or deleted providing a cdc4 polypeptide that can be produced by recombinant techniques and retains its activity, for example its ability to associate with a CPD motif.

[0212] In an aspect a cdc4 sequence is mutated by deleting the region from the beginning of the F-box domain to the end of the WD40 repeat domain. In particular, terminal residues 1 to 262 and 745 to 779 can be deleted from the cdc4 seqeunce.

[0213] Other additions, substitutions, and/or deletions may be made to the cdc4 mutants of the present invention. In an embodiment cdc4 can be engineered to remove flexible loops comprising residues 601 to 604 and 609 to 624.

[0214] Particular mutant cdc4 polypeptides of the invention are also identified in Table 5.

[0215] The present invention also relates to nucleic acid molecules or polynucleotides encoding a cdc4 mutant polypeptide. The polynucleotides can be used to transform host cells to express the cdc4 mutant polypeptides of the invention. They can also be used as a probe to detect related enzymes.

[0216] The present invention still further relates to recombinant vectors that include the nucleic acid molecules of the invention. The nucleic acid molecules of the invention may be inserted into an appropriate vector, and the vector may contain the necessary elements for the transcription and translation of an inserted coding sequence. Accordingly, vectors may be constructed which comprise a nucleic acid molecule of the invention, and where appropriate one or more transcription and translation elements linked to the nucleic acid molecule. A vector can be used to transform host cells. Therefore, the invention provides host cells containing a vector of the invention. As well, the invention provides methods of making such vectors and host cells.

[0217] The mutant cdc4 polypeptides of the invention can be encoded, expressed, and purified by any one of a number of methods known to those skilled in the art. Preferred production methods will depend on many factors including the costs and availability of materials and other economic considerations. The optimum production procedure for a given situation will be apparent to those skilled in the art through minimal experimentation.

[0218] In accordance with an aspect of the present invention, there is provided a process for producing a cdc4 mutant polypeptide by recombinant techniques utilizing the nucleic acid molecules of the invention. The method may comprise culturing recombinant host cells containing a nucleic acid sequence encoding a cdc4 mutant polypeptide, under conditions promoting expression of the cdc4 mutant polypeptide, and subsequent recovery of the cdc4 mutant polypeptide.

[0219] The invention further broadly contemplates a recombinant cdc4 mutant polypeptide obtained using a method of the invention.

[0220] A cdc4 mutant polypeptide of the invention may be conjugated with other molecules, such as polypeptides, to prepare fusion polypeptides or chimeric polypeptides. This may be accomplished, for example, by the synthesis of N-terminal or C-terminal fusion polypeptides.

[0221] The invention further contemplates antibodies having specificity against a cdc4 mutant polypeptide of the invention. Antibodies may be labeled with a detectable substance and used to detect cdc4 mutant polypeptides. In another embodiment, the invention provides an isolated antibody that binds specifically to a cdc4 mutant polypeptide.

[0222] The cdc4 mutant polypeptides of the present invention are particularly well suited for use in screening methods for identifying modulators of cdc4 or SCF complexes.

[0223] Still further the invention provides a method for evaluating a test compound for its ability to modulate the biological activity of a cdc4 polypepide. In this application, “modulate” refers to a change or an alteration in the biological activity of a cdc4 polypeptide. Modulation may be an increase or a decrease in activity, a change in characteristics (e.g. kinetic characteristics), or any other change in the biological, functional, or immunological properties of the polypeptide.

[0224] The substances and compounds identified using the methods of the invention, may be used to modulate the biological activity of a cdc4 polypeptide or a SCF complex, and they may be used in the treatment of conditions mediated by a cdc4 polypeptide or SCF complex. Accordingly, the substances and compounds may be formulated into compositions for administration to individuals suffering from one or more of these conditions. Therefore, the present invention also relates to a composition comprising one or more of a substance or compound identified using a method of the invention, and a pharmaceutically acceptable carrier, excipient or diluent. A method for treating or preventing these conditions is also provided comprising administering to a patient in need thereof, a composition of the invention.

[0225] Model

[0226] A crystal structure of the present invention may be used to make a model of a binding pocket of a SCF E3 ubiquitin ligase, in particular an F-box protein, that is involved in substrate selection and/or orientation. A model may, for example, be a structural model or a computer model. A model may represent the secondary, tertiary and/or quaternary structure of the binding pocket. The model itself may be in two or three dimensions. It is possible for a computer model to be in three dimensions despite the constraints imposed by a conventional computer screen, if it is possible to scroll along at least a pair of axes, causing “rotation” of the image.

[0227] As used herein, the term “modelling” includes the quantitative and qualitative analysis of molecular structure and/or function based on atomic structural information and interaction models. The term “modelling” includes conventional numeric-based molecular dynamic and energy minimization models, interactive computer graphic models, modified molecular mechanics models, distance geometry and other structure-based constraint models.

[0228] Preferably, modelling is performed using a computer and may be further optimized using known methods. This is called modelling optimisation.

[0229] An integral step to an approach of the invention for designing modulators (e.g. inhibitors) of a subject F-box protein or SCF complex involves construction of computer graphics models of a binding pocket of the invention which can be used to design pharmacophores by rational drug design. For instance, for an inhibitor to interact optimally with the subject binding pocket, it will generally be desirable that it have a shape which is at least partly complimentary to that of a particular binding pocket of the protein, as for example those binding pockets of the protein which are involved in recognition of a ligand (e.g. substrate). Additionally, other factors, including electrostatic interactions, hydrogen bonding, hydrophobic interactions, desolvation effects, and cooperative motions of ligand and receptor, all influence the binding effect and should be taken into account in attempts to design bioactive modulators (e.g. inhibitors).

[0230] As described herein, a computer-generated molecular model of the subject binding pockets can be created. In preferred embodiments, at least the Cα-carbon positions of the binding pockets are mapped to a particular coordinate pattern, such as the coordinates for a binding pocket in Table 6, by homology modeling, and the structure of the protein and velocities of each atom are calculated at a simulation temperature (T_(o)) at which the docking simulation is to be determined. Typically, such a protocol involves primarily the prediction of side-chain conformations in the modeled binding pocket, while assuming a main-chain trace taken from a tertiary structure such as provided in Table 6 and the Figures. Computer programs for performing energy minimization routines are commonly used to generate molecular models. For example, both the CHARMM (Brooks et al. (1983) J Comput Chem 4:187-217) and AMBER (Weiner et al (1981) J. Comput. Chem. 106: 765) algorithms handle all of the molecular system setup, force field calculation, and analysis (see also, Eisenfield et al. (1991) Am J Physiol 261:C376-386; Lybrand (1991) J Pharm Belg 46:49-54; Froimowitz (1990) Biotechniques 8:640-644; Burbam et al. (1990) Proteins 7:99-111; Pedersen (1985) Environ Health Perspect 61:185-190; and Kini et al. (1991) J Biomol Struct Dyn 9:475-488). At the heart of these programs is a set of subroutines that, given the position of every atom in the model, calculate the total potential energy of the system and the force on each atom. These programs may utilize a starting set of atomic coordinates, such as the coordinates provided in Table 6, the parameters for the various terms of the potential energy function, and a description of the molecular topology (the covalent structure). Common features of such molecular modeling methods include: provisions for handling hydrogen bonds and other constraint forces; the use of periodic boundary conditions; and provisions for occasionally adjusting positions, velocities, or other parameters in order to maintain or change temperature, pressure, volume, forces of constraint, or other externally controlled conditions.

[0231] Most conventional energy minimization methods use the input data described above and the fact that the potential energy function is an explicit, differentiable function of Cartesian coordinates, to calculate the potential energy and its gradient (which gives the force on each atom) for any set of atomic positions. This information can be used to generate a new set of coordinates in an effort to reduce the total potential energy and, by repeating this process over and over, to optimize the molecular structure under a given set of external conditions. These energy minimization methods are routinely applied to molecules similar to the subject proteins as well as nucleic acids, polymers and zeolites.

[0232] In general, energy minimization methods can be carried out for a given temperature, T_(is), which may be different than the docking simulation temperature, T_(o). Upon energy minimization of the molecule at T_(i), coordinates and velocities of all the atoms in the system are computed. Additionally, the normal modes of the system are calculated. It will be appreciated by those skilled in the art that each normal mode is a collective, periodic motion, with all parts of the system moving in phase with each other, and that the motion of the molecule is the superposition of all normal modes. For a given temperature, the mean square amplitude of motion in a particular mode is inversely proportional to the effective force constant for that mode, so that the motion of the molecule will often be dominated by the low frequency vibrations.

[0233] After the molecular model has been energy minimized at T_(i), the system is “heated” or “cooled” to the simulation temperature, T_(i), by carrying out an equilibration run where the velocities of the atoms are scaled in a step-wise manner until the desired temperature, T_(o), is reached. The system is further equilibrated for a specified period of time until certain properties of the system, such as average kinetic energy, remain constant. The coordinates and velocities of each atom are then obtained from the equilibrated system.

[0234] Further energy minimization routines can also be carried out. For example, a second class of methods involves calculating approximate solutions to the constrained EOM for the protein. These methods use an iterative approach to solve for the Lagrange multipliers and, typically, only need a few iterations if the corrections required are small. The most popular method of this type, SHAKE (Ryckaert et al. (1977) J Comput Phys 23:327; and Van Gunsteren et al. (1977) Mol Phys 34:13 11) is easy to implement and scales as O(N) as the number of constraints increases. Therefore, the method is applicable to macromolecules such as F-box proteins. An alternative method, RATTLE (Anderson (1983) J Comput Phys 52:24) is based on the velocity version of the Verlet algorithm. Like SHAKE, RATTLE is an iterative algorithm and can be used to energy minimize the model of the subject protein.

[0235] Overlays and super positioning with a three dimensional model of a binding pocket of the invention may be used for modelling optimisation. Additionally alignment and/or modelling can be used as a guide for the placement of mutations on a binding pocket to characterize the nature of the site in the context of a cell.

[0236] The three dimensional structure of a new crystal may be modelled using molecular replacement. The term “molecular replacement” refers to a method that involves generating a preliminary model of a molecule or complex whose structural coordinates are unknown, by orienting and positioning a molecule whose structural coordinates are known within the unit cell of the unknown crystal, so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal. Lattman, E., “Use of the Rotation and Translation Functions”, in Methods in Enzymology, 115, pp. 55-77 (1985); M. G. Rossmann, ed., “The Molecular Replacement Method”, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York, (1972).

[0237] Commonly used computer software packages for molecular replacement are X-PLOR (Brunger 1992, Nature 355: 472-475), AMoRE (Navaza, 1994, Acta Crystallogr. A50:157-163), the CCP4 package (Collaborative Computational Project, Number 4, “The CCP4 Suite: Programs for Protein Crystallography”, Acta Cryst., Vol. D50, pp. 760-763, 1994), the MERLOT package (P. M. D. Fitzgerald, J. Appl. Cryst., Vol. 21, pp. 273-278, 1988) and XTALVIEW (McCree et al (1992) J. Mol. Graphics 10: 44-46. It is preferable that the resulting structure not exhibit a root-mean-square deviation of more than 3 Å.

[0238] Molecular replacement computer programs generally involve the following steps: (1) determining the number of molecules in the unit cell and defining the angles between them (self rotation function); (2) rotating the known structure against diffraction data to define the orientation of the molecules in the unit cell (rotation function); (3) translating the known structure in three dimensions to correctly position the molecules in the unit cell (translation function); (4) determining the phases of the X-ray diffraction data and calculating an R-factor calculated from the reference data set and from the new data wherein an R-factor between 30-50% indicates that the orientations of the atoms in the unit cell have been reasonably determined by the method; and (5) optionally, decreasing the R-factor to about 20% by refining the new electron density map using iterative refinement techniques known to those skilled in the art (refinement).

[0239] The quality of the model may be analysed using a program such as PROCHECK or 3D-Profiler [Laskowski et al 1993 J. Appl. Cryst. 26:283-291; Luthy R. et al, Nature 356: 83-85, 1992; and Bowie, J. U. et al, Science 253: 164-170, 1991]. Once any irregularities have been resolved, the entire structure may be further refined.

[0240] Other molecular modelling techniques may also be employed in accordance with this invention. See, e.g., Cohen, N. C. et al, “Molecular Modelling Software and Methods for Medicinal Chemistry”, J. Med. Chem., 33, pp. 883-894 (1990). See also, Navia, M. A. and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202-210 (1992).

[0241] Using the structural coordinates of crystal provided by the invention, molecular modelling may be used to determine the structural coordinates of a crystalline mutant or homolog of a SCF complex or F-box binding pocket involved in substrate selection and/or orientation. By the same token a crystal of the invention can be used to provide a model of a substrate or ligand. Modelling techniques can then be used to approximate the three dimensional structure of substrate or ligand derivatives and other components which may be able to mimic the atomic contacts between a substrate or ligand and binding pocket.

[0242] Computer Format of Crystals/Models

[0243] Information derivable from a crystal of the present invention (for example the structural coordinates) and/or the model of the present invention may be provided in a computer-readable format.

[0244] Therefore, the invention provides a computer readable medium or a machine readable storage medium which comprises the structural coordinates of a binding pocket of an SCF complex of F box protein described herein including all or any parts thereof, or substrates or ligands including portions thereof. Such storage medium or storage medium encoded with these data are capable of displaying on a computer screen or similar viewing device, a three-dimensional graphical representation of a molecule or molecular complex which comprises such binding pockets or similarly shaped homologous binding pockets. Thus, the invention also provides computerized representations of the secondary or three-dimensional structures of a binding pocket of the invention, including any electronic, magnetic, or electromagnetic storage forms of the data needed to define the structures such that the data will be computer readable for purposes of display and/or manipulation.

[0245] In an aspect the invention provides a computer for producing a three-dimensional representation of a molecule or molecular complex, wherein said molecule or molecular complex comprises a binding pocket defined by structural coordinates of a binding pocket or structural coordinates of atoms of a substrate or ligand, or a three-dimensional representation of a homolog of said molecule or molecular complex, wherein said homolog comprises a binding pocket, or substrate or ligand that has a root mean square deviation from the backbone atoms not more than 1.5 angstroms wherein said computer comprises:

[0246] (a) a machine-readable data storage medium comprising a data storage material encoded with machine readable data wherein said data comprises the structural coordinates of a binding pocket or a substrate according to Table 6;

[0247] (b) a working memory for storing instructions for processing said machine-readable data;

[0248] (c) a central-processing unit coupled to said working memory and to said machine-readable data storage medium for processing said machine readable data into said three-dimensional representation; and

[0249] (d) a display coupled to said central-processing unit for displaying said three-dimensional representation.

[0250] The invention also provides a computer for determining at least a portion of the structural coordinates corresponding to an X-ray diffraction pattern of a molecule or molecular complex wherein said computer comprises:

[0251] (a) a machine-readable data storage medium comprising a data storage material encoded with machine readable data wherein said data comprises the structural coordinates according to Table 6;

[0252] (b) a machine-readable data storage medium comprising a data storage material encoded with machine readable data wherein said data comprises an X-ray diffraction pattern of said molecule or molecular complex;

[0253] (c) a working memory for storing instructions for processing said machine-readable data of (a) and (b);

[0254] (d) a central-processing unit coupled to said working memory and to said machine-readable data storage medium of (a) and (b) for performing a Fourier transform of the machine readable data of (a) and for processing said machine readable data of (b) into structural coordinates; and

[0255] (e) a display coupled to said central-processing unit for displaying said structural coordinates of said molecule or molecular complex.

[0256] Structural Studies

[0257] The present invention also provides a method for determining the secondary and/or tertiary structures of a pol)peptide or part or complexes thereof by using a crystal, or a model according to the present invention. The polypeptide or part thereof may be any polypeptide or part thereof for which the secondary and or tertiary structure is uncharacterised or incompletely characterised. In a preferred embodiment the polypeptide shares (or is predicted to share) some structural or functional homology to a crystal of the present invention. For example, the polypeptide may show a degree of structural homology over some or all parts of the primary amino acid sequence.

[0258] The polypeptide may be an F-box protein, or part thereof with a different specificity for a substrate. Alternatively (or in addition) the polypeptide may be an F-box protein from a different species.

[0259] The polypeptide may be a mutant of a wild-type F-box protein. A mutant may arise naturally, or may be made artificially (for example using molecular biology techniques). The mutant may also not be “made” at all in the conventional sense, but merely tested theoretically using the model of the present invention. A mutant may or may not be functional.

[0260] Thus, using a model of the present invention, the effect of a particular mutation on the overall two and/or three dimensional structure of an F-box protein or SCF complex or the interaction between a binding pocket of an F-box protein or SCF complex and a substrate or ligand can be investigated.

[0261] Alternatively, the polypeptide may perform an analogous function or be suspected to show a similar mechanism to an F-box protein.

[0262] The polypeptide may also be the same as the polypeptide of the crystal, but in association with a different substrate or ligand (for example, modulator or inhibitor) or cofactor. In this way it is possible to investigate the effect of altering the substrate or ligand with which the polypeptide is associated on the structure of the binding pocket.

[0263] Secondary or tertiary structure may be determined by applying the structural coordinates of a crystal or model of the present invention to other data such as an amino acid sequence, X-ray crystallographic diffraction data, or nuclear magnetic resonance (NMR) data. Homology modeling, molecular replacement, and nuclear magnetic resonance methods using these other data sets are described below.

[0264] Homology modeling (also known as comparative modeling or knowledge-based modeling) methods develop a three dimensional model from a polypeptide sequence based on the structures of known proteins (i.e. an F-box structure or complex thereof described herein). The method utilizes a computer model of a crystal of the present invention (the “known structure”), a computer representation of the amino acid sequence of the polypeptide with an unknown structure, and standard computer representations of the structures of amino acids. The method in particular comprises the steps of; (a) identifying structurally conserved and variable regions in the known structure; (b) aligning the amino acid sequences of the known structure and unknown structure (c) generating co-ordinates of main chain atoms and side chain atoms in structurally conserved and variable regions of the unknown structure based on the coordinates of the known structure thereby obtaining a homology model; and (d) refining the homology model to obtain a three dimensional structure for the unknown structure. This method is well known to those skilled in the art (Greer, 1985, Science 228, 1055; Bundell et al 1988, Eur. J. Biochem. 172, 513; Knighton et al., 1992, Science 258:130-135, http://biochem.vt.edu/courses/modeling/homology.htn). Computer programs that can be used in homology modelling are Quanta and the Homology module in the Insight II modelling package distributed by Molecular Simulations Inc, or MODELLER (Rockefeller University, www.iucr.ac.uk/sinris-top/logical/prg-modeller.html).

[0265] In step (a) of the homology modelling method, a known structure is examined to identify the structurally conserved regions (SCRs) from which an average structure, or framework, can be constructed for these regions of the protein. Variable regions (VRs), in which known structures may differ in conformation, also must be identified. SCRs generally correspond to the elements of secondary structure, such as alpha-helices and beta-sheets, and to ligand- and substrate-binding sites. The VRs usually lie on the surface of the proteins and form the loops where the main chain turns.

[0266] Many methods are available for sequence alignment of known structures and unknown structures. Sequence alignments generally are based on the dynamic programming algorithm of Needleman and Wunsch [J. Mol. Biol. 48: 442-453, 1970]. Current methods include FASTA, Smith-Waterman, and BLASTP, with the BLASTP method differing from the other two in not allowing gaps. Scoring of alignments typically involves construction of a 20×20 matrix in which identical amino acids and those of similar character (i.e., conservative substitutions) may be scored higher than those of different character. Substitution schemes which may be used to score alignments include the scoring matrices PAM (Dayhoff et al., Meth. Enzymol. 91: 524-545, 1983), and BLOSUM (Henikoff and Henikoff, Proc. Nat. Acad. Sci. USA 89: 10915-0919, 1992), and the matrices based on alignments derived from three-dimensional structures including that of Johnson and Overington (JO matrices) (J. Mol. Biol. 233: 716-738, 1993).

[0267] Alignment based solely on sequence may be used; however, other structural features also may be taken into account. In Quanta, multiple sequence alignment algorithms are available that may be used when aligning a sequence of the unknown with the known structures. Four scoring systems (i.e. sequence homology, secondary structure homology, residue accessibility homology, CA-CA distance homology) are available, each of which may be evaluated during an alignment so that relative statistical weights may be assigned.

[0268] When generating coordinates for the unknown structure, main chain atoms and side chain atoms, both in SCRs and VRs need to be modelled. A variety of approaches known to those skilled in the art may be used to assign co-ordinates to the unknown. In particular, the co-ordinates of the main chain atoms of SCRs will be transferred to the unknown structure. VRs correspond most often to the loops on the surface of the polypeptide and if a loop in the known structure is a good model for the unknown, then the main chain co-ordinates of the known structure may be copied. Side chain coordinates of SCRs and VRs are copied if the residue type in the unknown is identical to or very similar to that in the known structure. For other side chain coordinates, a side chain rotamer library may be used to define the side chain coordinates. When a good model for a loop cannot be found fragment databases may be searched for loops in other proteins that may provide a suitable model for the unknown. If desired, the loop may then be subjected to conformational searching to identify low energy conformers if desired.

[0269] Once a homology model has been generated it is analyzed to determine its correctness. A computer program available to assist in this analysis is the Protein Health module in Quanta which provides a variety of tests. Other programs that provide structure analysis along with output include PROCHECK and 3D-Profiler [Luthy R. et al, Nature 356: 83-85, 1992; and Bowie, J. U. et al, Science 253: 164-170, 1991]. Once any irregularities have been resolved, the entire structure may be further refined. Refinement may consist of energy minimization with restraints, especially for the SCRs. Restraints may be gradually removed for subsequent minimizations. Molecular dynamics may also be applied in conjunction with energy minimization.

[0270] Molecular replacement involves applying a known structure to solve the X-ray crystallographic data set of a polypeptide of unknown structure. The method can be used to define the phases describing the X-ray diffraction data of a polypeptide of unknown structure when only the amplitudes are known. Thus in an embodiment of the invention, a method is provided for determining three dimensional structures of polypeptides with unknown structure by applying the structural coordinates of a crystal of the present invention to provide an X-ray crystallographic data set for a polypeptide of unknown structure, and (b) determining a low energy conformation of the resulting structure.

[0271] The structural coordinates of a crystal of the present invention may be applied to nuclear magnetic resonance (NMR) data to determine the three dimensional structures of polypeptides with uncharacterised or incompletely characterised sturcture. (See for example, Wuthrich, 1986, John Wiley and Sons, New York: 176-199; Pflugrath et al., 1986, J. Molecular Biology 189: 383-386; Kline et al., 1986 J. Molecular Biology 189:377-382). While the secondary structure of a polypeptide may often be determined by NMR data, the spatial connections between individual pieces of secondary structure are not as readily determined. The structural coordinates of a polypeptide defined by X-ray crystallography can guide the NMR spectroscopist to an understanding of the spatial interactions between secondary structural elements in a polypeptide of related structure. Information on spatial interactions between secondary structural elements can greatly simplify Nuclear Overhauser Effect (NOE) data from two-dimensional NMR experiments. In addition, applying the structural coordinates after the determination of secondary structure by NMR techniques simplifies the assignment of NOE's relating to particular amino acids in the polypeptide sequence and does not greatly bias the NMR analysis of polypeptide structure.

[0272] In an embodiment, the invention relates to a method of determining three dimensional structures of polypeptides with unknown structures, by applying the structural coordinates of a crystal of the present invention to nuclear magnetic resonance (NMR) data of the unknown structure. This method comprises the steps of: (a) determining the secondary structure of an unknown structure using NMR data; and (b) simplifying the assignment of through-space interactions of amino acids. The term “through-space interactions” defines the orientation of the secondary structural elements in the three dimensional structure and the distances between amino acids from different portions of the amino acid sequence. The term “assignment” defines a method of analyzing NMR data and identifying which amino acids give rise to signals in the NMR spectrum.

[0273] Screening Methods

[0274] Another aspect of the present invention is the design and identification of agents that inhibit or potentiate an interaction between an F-box protein or an SCF E3 ubiquitin ligase and a substrate. The rationale design and identification of agents can be accomplished by utilizing the structural coordinates that define a binding pocket of the present invention involved in substrate selection and/or orientation.

[0275] The structures described herein, and the structures of other polypeptides determined by homology modeling, molecular replacement, and NMR techniques described herein can also be applied to modulator design and identification methods.

[0276] The invention contemplates molecular models, in particular three-dimensional molecular models of binding pockets of the present invention involved in substrate selection and/or orientation, and their use as templates for the design of agents able to mimic or inhibit substrate binding (e.g. modulators).

[0277] In certain embodiments, the present invention provides a method of screening for a ligand that associates with a binding pocket and/or modulates the function of a F-box protein or SCF complex by using a crystal or a model according to the present invention. The method may involve investigating whether a test compound is capable of associating with or binding a binding pocket, and/or inhibiting or enhancing interactions of atomic contacts in a binding pocket.

[0278] In accordance with an aspect of the present invention, a method is provided for screening for a ligand capable of binding to a binding pocket, wherein the method comprises using a crystal or model according to the invention.

[0279] In another aspect, the invention relates to a method of screening for a ligand capable of binding to a binding pocket, wherein the binding pocket is defined by the structural coordinates given herein, the method comprising contacting the binding pocket with a test compound and determining if the test compound binds to the binding pocket.

[0280] In one embodiment, the present invention provides a method of screening for a test compound capable of interacting with one or more key amino acid residues of a binding pocket of the present invention. For example, a test compound that interacts with one or more of amino acids of a binding pocket may prevent interaction of the F-box protein or complex thereof and its substrate resulting in modification of the SCF E3 ubiquitin ligase activity.

[0281] Another aspect of the invention provides a process comprising the steps of:

[0282] (a) performing a method of screening for a ligand described above;

[0283] (b) identifying one or more ligands capable of binding to a binding pocket; and

[0284] (c) preparing a quantity of said one or more ligands.

[0285] A further aspect of the invention provides a process comprising the steps of;

[0286] (a) performing a method of screening for a ligand as described above;

[0287] (b) identifying one or more ligands capable of binding to a binding pocket; and

[0288] (c) preparing a pharmaceutical composition comprising said one or more ligands.

[0289] Once a test compound capable of interacting with one or more key amino acid residues in a binding pocket of the present invention has been identified, further steps may be carried out either to select and/or modify compounds and/or to modify existing compounds, to modulate the interaction with the key amino acid residues in the binding pocket.

[0290] Yet another aspect of the invention provides a process comprising the steps of;

[0291] (a) performing the method of screening for a ligand as described above;

[0292] (b) identifying one or more ligands capable of binding to a binding pocket;

[0293] (c) modifying said one or more ligands capable of binding to a binding pocket;

[0294] (d) performing said method of screening for a ligand as described above; and

[0295] (e) optionally preparing a pharmaceutical composition comprising said one or more ligands.

[0296] In another aspect of the invention, a method of screening for a test compound is provided comprising screening for test compounds that affect (inhibit or potentiate) an interaction between an F-box protein or SCF complex and a substrate as defined by interactions 1 to 4 or 5 to 8/9 in Table 3 or Table 4.

[0297] As used herein, the term “test compound” means any compound which is potentially capable of associating with a binding pocket, inhibiting or enhancing interactions of atomic contacts in a binding pocket. If, after testing, it is determined that the test compound does bind to the binding pocket, inhibits or enhances interactions of atomic contacts in a binding pocket, it is known as a “ligand”.

[0298] The test compound may be designed or obtained from a library of compounds which may comprise peptides, as well as other compounds, such as small organic molecules and particularly new lead compounds. By way of example, the test compound may be a natural substance, a biological macromolecule, or an extract made from biological materials such as bacteria, fungi, or animal (particularly mammalian) cells or tissues, an organic or an inorganic molecule, a synthetic test compound, a semi-synthetic test compound, a carbohydrate, a monosaccharide, an oligosaccharide or polysaccharide, a glycolipid, a glycopeptide, a saponin, a heterocyclic compound, a structural or functional mimetic, a peptide, a peptidomimetic, a derivatised test compound, a peptide cleaved from a whole protein, or a peptide synthesised synthetically (such as, by way of example, either using a peptide synthesizer or by recombinant techniques or combinations thereof), a recombinant test compound, a natural or a non-natural test compound, a fusion protein or equivalent thereof and mutants, derivatives or combinations thereof.

[0299] The increasing availability of biomacromolecule structures of potential pharmacophoric molecules that have been solved crystallographically has prompted the development of a variety of direct computational methods for molecular design, in which the steric and electronic properties of substrate binding sites are use to guide the design of potential ligands (Cohen et al. (1990) J. Med. Cam. 33: 883-894; Kuntz et al. (1982) J. Mol. Biol 161: 269-288; DesJarlais (1988) J. Med. Cam. 31: 722-729; Bartlett et al. (1989) (Spec. Publ., Roy. Soc. Chem.) 78: 182-196; Goodford et al. (1985) J. Med. Cam. 28: 849-857; DesJarlais et al. J. Med. Cam. 29: 2149-2153). Directed methods generally fall into two categories: (1) design by analogy in which 3-D structures of known molecules (such as from a crystallographic database) are docked to the structure and scored for goodness-of-fit; and (2) de novo design, in which the ligand model is constructed piece-wise. The latter approach, in particular, can facilitate the development of novel molecules, uniquely designed to bind to the subject binding pockets.

[0300] The test compound may be screened as part of a library or a data base of molecules. Modulators of a binding pocket of the present invention may be identified by docking a computer representation of compounds from one or more database of molecules. Data bases which may be used include ACD (Molecular Designs Limited), NCI (National Cancer Institute), CCDC (Cambridge Crystallographic Data Center), CAST (Chemical Abstract Service), Derwent (Derwent Information Limited), Maybridge (Maybridge Chemical Company Ltd), Aldrich (Aldrich Chemical Company), DOCK (University of California in San Francisco), and the Directory of Natural Products (Chapman & Hall). Computer programs such as CONCORD (Tripos Associates) or DB-Converter (Molecular Simulations Limited) can be used to convert a data set represented in two dimensions to one represented in three dimensions.

[0301] Test compounds may tested for their capacity to fit spatially into a binding pocket. As used herein, the term “fits spatially” means that the three-dimensional structure of the test compound is accommodated geometrically in a cavity of a binding pocket. The test compound can then be considered to be a ligand.

[0302] A favourable geometric fit occurs when the surface area of the test compound is in close proximity with the surface area of the cavity of a binding pocket without forming unfavorable interactions. A favourable complementary interaction occurs where the test compound interacts by hydrophobic, aromatic, ionic, dipolar, or hydrogen donating and accepting forces. Unfavourable interactions may be steric hindrance between atoms in the test compound and atoms in the binding pocket.

[0303] If a model of the present invention is a computer model, the test compounds may be positioned in a binding pocket through computational docking. If, on the other hand, the model of the present invention is a structural model, the test compounds may be positioned in the binding pocket by, for example, manual docking.

[0304] As used herein the term “docking” refers to a process of placing a compound in close proximity with a binding pocket, or a process of finding low energy conformations of a test compound/binding pocket complex.

[0305] A screening method of the present invention may comprise the following steps:

[0306] (i) generating a computer model of a binding pocket using a crystal according to the invention;

[0307] (ii) docking a computer representation of a test compound with the computer model; and

[0308] (iii) analysing the fit of the compound in the binding pocket.

[0309] In an aspect of the invention, a method is provided comprising the following steps:

[0310] (a) docking a computer representation of a structure of a test compound into a computer representation of a binding pocket defined in accordance with the invention using a computer program, or by interactively moving the representation of the test compound into the representation of the binding pocket;

[0311] (b) characterizing the geometry and the complementary interactions formed between the atoms of the binding pocket and the compound; optionally

[0312] (c) searching libraries for molecular fragments which can fit into the empty space between the compound and the binding pocket and can be linked to the compound; and

[0313] (d) linking the fragments found in (c) to the compound and evaluating the new modified compound.

[0314] In an embodiment of the invention, a method is provided which comprises the following steps:

[0315] (a) docking a computer representation of a test compound from a computer data base with a computer representation of a selected binding pocket defined in accordance with the invention to define a complex;

[0316] (b) determining a conformation of the complex with a favorable fit and favourable complementary interactions; and

[0317] (c) identifying test compounds that best fit the selected binding pocket as potential modulators of a F-box protein or SCF complex comprising the binding pocket.

[0318] In another embodiment of the invention, a method is provided which comprises docking a computer representation of a selected binding pocket defined by the atomic interactions, atomic contacts, or structural coordinates in accordance with the invention to define a complex. In particular a method is provided comprising:

[0319] (a) docking a computer representation of a test compound from a computer database with a computer representation of a selected binding pocket defined by the atomic interactions, atomic contacts, or structural coordinates described herein;

[0320] (b) determining a conformation of the complex with a favorable fit and favourable complementary interactions; and

[0321] (c) identifying test compounds that best fit the selected binding pocket as potential modulators of the a F-box protein or SCF complex comprising the binding pocket

[0322] A model used in a screening method may comprise a binding pocket either alone or in association with one or more ligands and/or cofactors. For example, the model may comprise the binding pocket in association with a substrate (or analogue thereof), and/or modulator.

[0323] If the model comprises an unassociated binding pocket, then the selected site under investigation may be the binding pocket itself. The test compound may, for example, mimic a known ligand (e.g. substrate) for an F-box protein in order to interact with the binding pocket. The selected site may alternatively be another site on the F-box protein.

[0324] If the model comprises an associated binding pocket, for example a binding pocket in association with a substrate or ligand, the selected site may be the binding pocket or a site made up of the binding pocket and the complexed substrate or ligand, or a site on the substrate or ligand itself. The test compound may be investigated for its capacity to modulate the interaction with the associated molecule.

[0325] The screening methods described herein may be applied to a plurality of test compounds, to identify those that best fit the selected site. A test compound (or plurality of test compounds) may be selected on the basis of their similarity to a substrate or ligand for an F-box protein. For example, the screening method may comprise the following steps:

[0326] (i) generating a computer model of a binding pocket in complex with a substrate or ligand;

[0327] (ii) searching for a test compound with a similar three dimensional structure and/or similar chemical groups as the substrate or ligand; and

[0328] (iii) evaluating the fit of the test compound in the binding pocket.

[0329] Searching may be carried out using a database of computer representations of potential compounds, using methods known in the art.

[0330] The present invention also provides a method for designing ligands for F-box proteins or SCF complexes. It is well known in the art to use a screening method as described above to identify a test compound with promising fit, but then to use this test compound as a starting point to design a ligand with improved fit to the model. Such techniques are known as “structure-based ligand design” (See Kuntz et al., 1994, Acc. Chem. Res. 27:117; Guida, 1994, Current Opinion in Struc. Biol. 4: 777; and Colman, 1994, Current Opinion in Struc. Biol. 4: 868, for reviews of structure-based drug design and identification; and Kuntz et al 1982, J. Mol. Biol. 162:269; Kuntz et al., 1994, Acc. Chem. Res. 27: 117; Meng et al., 1992, J. Compt. Chem. 13: 505; Bohm, 1994, J. Comp. Aided Molec. Design 8: 623 for methods of structure-based modulator design).

[0331] Examples of computer programs that may be used for structure-based ligand design are CAVEAT (Bartlett et al., 1989, in “Chemical and Biological Problems in Molecular Recognition”, Roberts, S. M. Ley, S. V.; Campbell, N. M. eds; Royal Society of Chemistry: Cambridge, pp 182-196); FLOG (Miller et al., 1994, J. Comp. Aided Molec. Design 8:153); PRO Modulator (Clark et al., 1995 J. Comp. Aided Molec. Design 9:13); MCSS (Miranker and Karplus, 1991, Proteins: Structure, Fuction, and Genetics 8:195); and, GRID (Goodford, 1985, J. Med. Chem. 28:849).

[0332] The method may comprise the following steps:

[0333] (i) docking a model of a test compound with a model of a binding pocket;

[0334] (ii) identifying one or more groups on the test compound which may be modified to improve their fit in the binding pocket;

[0335] (iii) replacing one or more identified groups to produce a modified test compound model; and

[0336] (iv) docking the modified test compound model with the model of the binding pocket.

[0337] Evaluation of fit may comprise the following steps:

[0338] (a) mapping chemical features of a test compound such as by hydrogen bond donors or acceptors, hydrophobic/lipophilic sites, positively ionizable sites, or negatively ionizable sites; and

[0339] (b) adding geometric constraints to selected mapped features.

[0340] The fit of the modified test compound may then be evaluated using the same criteria.

[0341] The chemical modification of a group may either enhance or reduce hydrogen bonding interaction, charge interaction, hydrophobic interaction, Van Der Waals interaction or dipole interaction between the test compound and the key amino acid residue(s) of the binding pocket. Preferably the group modifications involve the addition removal or replacement of substituents onto the test compound such that the substituents are positioned to collide or to bind preferentially with one or more amino acid residues that correspond to the key amino acid residues of the binding pocket.

[0342] If a modified test compound model has an improved fit, then it may bind to a binding pocket and be considered to be a “ligand”. Rational modification of groups may be made with the aid of libraries of molecular fragments which may be screened for their capacity to fit into the available space and to interact with the appropriate atoms. Databases of computer representations of libraries of chemical groups are available commercially, for this purpose.

[0343] The test compound may also be modified “in situ” (i.e. once docked into the potential binding pocket), enabling immediate evaluation of the effect of replacing selected groups. The computer representation of the test compound may be modified by deleting a chemical group or groups, or by adding a chemical group or groups. After each modification to a compound, the atoms of the modified compound and potential binding pocket can be shifted in conformation and the distance between the modulator and the binding pocket atoms may be scored on the basis of geometric fit and favourable complementary interactions between the molecules. This technique is described in detail in Molecular Simulations User Manual, 1995 in LUDI.

[0344] Examples of ligand building and/or searching computer programs include programs in the Molecular Simulations Package (Catalyst), ISIS/HOST, ISIS/BASE, and ISIS/DRAW (Molecular Designs Limited), and UNITY (Tripos Associates).

[0345] The “starting point” for rational ligand design may be a known substrate or lignad. For example, in order to identify potential modulators of an F-box protein, a logical approach would be to start with a known ligand or substrate to produce a molecule which mimics the binding of the ligand or substrate. Such a molecule may, for example, act as a competitive inhibitor for the true substrate or ligand, or may bind so strongly that the interaction (and inhibition) is effectively irreversible.

[0346] Such a method may comprise the following steps:

[0347] (i) generating a computer model of a binding pocket in complex with a substrate or ligand;

[0348] (ii) replacing one or more groups on the ligand model to produce a modified substrate or ligand; and

[0349] (iii) evaluating the fit of the modified substrate or ligand in the binding pocket.

[0350] The replacement groups could be selected and replaced using a compound construction program which replaces computer representations of chemical groups with groups from a computer database, where the representations of the compounds are defined by structural coordinates.

[0351] In an embodiment, a screening method is provided for identifying a substrate or ligand of an F-box protein, comprising the step of using the structural coordinates of a CPD motif defined in relation to its spatial association with a binding pocket of the invention, to generate a compound that is capable of associating with the binding pocket.

[0352] In an embodiment of the invention, a screening method is provided for identifying a ligand of an F-box protein, in particular a cdc4 protein, comprising the step of using the structural coordinates of the CPD motif listed in Table 6 to generate a compound for associating with a binding pocket of an F-box protein, in particular a cdc4 protein as described herein. The following steps are employed in a particular method of the invention: (a) generating a computer representation of a CPD motif defined by its structural coordinates listed in Table 6; and (b) searching for molecules in a data base that are structurally or chemically similar to the defined CPD motif, using a searching computer program, or replacing portions of the CPD motif with similar chemical structures from a database using a compound building computer program.

[0353] A screening method is provided for identifying a ligand of an F-box protein, in particular a cdc4 protein, or a SCF complex comprising the step of using the structural coordinates of a binding pocket comprising a WD40 repeat or part thereof listed in Table 6 to generate a compound for associating with a F-box domain of an F-box protein. The following steps are employed in a particular method of the invention: (a) generating a computer representation of a binding pocket comprising a WD40 repeat region or part thereof defined by its structural coordinates listed in Table 6; and (b) searching for molecules in a data base that are structurally or chemically similar to the defined binding pocket using a searching computer program, or replacing portions of the binding pocket with structures from a database using a compound building computer program.

[0354] A screening method is provided for identifying a ligand of an F-box protein, in particular a cdc4 protein, of a SCF complex comprising the step of using the structural coordinates of a binding pocket comprising an F-box domain or part thereof, or helical linker listed in Table 6 to generate a compound for associating with a F-box domain or helical linker of an F-box protein. The following steps are employed in a particular method of the invention: (a) generating a computer representation of a binding pocket comprising a an F-box domain or part thereof, or helical linker defined by its structural coordinates listed in Table 4; and (b) searching for molecules in a data base that are structurally or chemically similar to the defined binding pocket using a searching computer program, or replacing portions of the binding pocket with structures from a database using a compound building computer program.

[0355] The screening methods of the present invention may be used to identify compounds or entities that associate with a molecule that associates with an F-box protein, in particular a cdc4 protein, or an SCF complex.

[0356] In an illustrative embodiment, the design of potential modulators or substrates for SCF complexes begins from the general perspective of shape complimentarity for an active site and substrate specificity subsites of the receptor, and a search algorithm is employed which is capable of scanning a database of small molecules of known three-dimensional structure for candidates which fit geometrically into the target protein site. It is not expected that the molecules found in the shape search will necessarily be leads themselves, since no evaluation of chemical interaction need necessarily be made during the initial search. Rather, it is anticipated that such candidates might act as the framework for further design, providing molecular skeletons to which appropriate atomic replacements can be made. Of course, the chemical complimentarity of these molecules can be evaluated, but it is expected that atom types will be changed to maximize the electrostatic, hydrogen bonding, and hydrophobic interactions with the receptor. Most algorithms of this type provide a method for finding a wide assortment of chemical structures that are complementary to the shape of a binding site of a subject molecule or complex. Each of a set of small molecules from a particular data-base, such as the Cambridge Crystallographic Data Bank (CCDB) (Allen et al. (1973) J. Chem. Doc. 13: 119), is individually docked to the binding pocket of the invention, in a number of geometrically permissible orientations with use of a docking algorithm. In a preferred embodiment, a set of computer algorithms called DOCK, can be used to characterize the shape of invaginations and grooves that form active sites and recognition surfaces of a subject molecule or complex (Kuntz et al. (1982) J. Mol. Biol 161: 269-288). The program can also search a database of small molecules for templates whose shapes are complementary to particular binding pockets or sites of a receptor (DesJarlais et al. (1988) J Med Chem 31: 722-729). These templates normally require modification to achieve good chemical and electrostatic interactions (DesJarlais et al. (1989) ACS Symp Ser 413: 60-69). However, the program has been shown to position accurately known cofactors for ligands based on shape constraints alone.

[0357] The orientations are evaluated for goodness-of-fit and the best are kept for further examination using molecular mechanics programs, such as AMBER or CHARMM. Such algorithms have previously proven successful in finding a variety of molecules that are complementary in shape to a given binding site of a molecule or complex, and have been shown to have several attractive features. First, such algorithms can retrieve a remarkable diversity of molecular architectures. Second, the best structures have, in previous applications to other proteins, demonstrated impressive shape complementarity over an extended surface area. Third, the overall approach appears to be quite robust with respect to small uncertainties in positioning of the candidate atoms.

[0358] Goodford (1985, J Med Chem 28:849-857) and Boobbyer et al. (1989, J Med Chem 32:1083-1094) have produced a computer program (GRID) which seeks to determine regions of high affinity for different chemical groups (termed probes) on the molecular surface of the binding site. GRID hence provides a tool for suggesting modifications to known ligands that might enhance binding. It may be anticipated that some of the sites discerned by GRID as regions of high affinity correspond to “pharmacophoric patterns” determined inferentially from a series of known ligands. As used herein, a pharmacophoric pattern is a geometric arrangement of features of the anticipated ligand that is believed to be important for binding. Attempts have been made to use pharmacophoric patterns as a search screen for novel ligands (Jakes et al. (1987) J Mol Graph 5:41-48; Brint et al. (1987) J Mol Graph 5:49-56; Jakes et al. (1986) J Mol Graph 4:12-20); however, the constraint of steric and “chemical” fit in the putative (and possibly unknown) binding pocket or site is ignored. Goodsell and Olson (1990, Proteins: Struct Funct Genet 8:195-202) have used the Metropolis (simulated annealing) algorithm to dock a single known ligand into a target protein. They allow torsional flexibility in the ligand and use GRID interaction energy maps as rapid lookup tables for computing approximate interaction energies. Given the large number of degrees of freedom available to the ligand, the Metropolis algorithm is time-consuming and is unsuited to searching a candidate database of a few thousand small molecules.

[0359] Yet a further embodiment of the present invention utilizes a computer algorithm such as CLIX which searches such databases as CCDB for small molecules which can be oriented in a binding pocket or site in a way that is both sterically acceptable and has a high likelihood of achieving favorable chemical interactions between the candidate molecule and the surrounding amino acid residues. The method is based on characterizing a binding pocket in terms of an ensemble of favorable binding positions for different chemical groups and then searching for orientations of the candidate molecules that cause maximum spatial coincidence of individual candidate chemical groups with members of the ensemble. The current availability of computer power dictates that a computer-based search for novel ligands follows a breadth-first strategy. A breadth-first strategy aims to reduce progressively the size of the potential candidate search space by the application of increasingly stringent criteria, as opposed to a depth-first strategy wherein a maximally detailed analysis of one candidate is performed before proceeding to the next. CLIX conforms to this strategy in that its analysis of binding is rudimentary—it seeks to satisfy the necessary conditions of steric fit and of having individual groups in “correct” places for bonding, without imposing the sufficient condition that favorable bonding interactions actually occur. A ranked “shortlist” of molecules, in their favored orientations, is produced which can then be examined on a molecule-by-molecule basis, using computer graphics and more sophisticated molecular modeling techniques. CLIX is also capable of suggesting changes to the substituent chemical groups of the candidate molecules that might enhance binding.

[0360] The algorithmic details of CLIX is described in Lawerence et al. (1992) Proteins 12:31-41, and the CLIX algorithm can be summarized as follows. The GRID program is used to determine discrete favorable interaction positions (termed target sites) in the binding pocket or site of the protein for a wide variety of representative chemical groups. For each candidate ligand in the CCDB an exhaustive attempt is made to make coincident, in a spatial sense in the binding site of the protein, a pair of the candidate's substituent chemical groups with a pair of corresponding favorable interaction sites proposed by GRID. All possible combinations of pairs of ligand groups with pairs of GRID sites are considered during this procedure. Upon locating such coincidence, the program rotates the candidate ligand about the two pairs of groups and checks for steric hindrance and coincidence of other candidate atomic groups with appropriate target sites. Particular candidate/orientation combinations that are good geometric fits in the binding site and show sufficient coincidence of atomic groups with GRID sites are retained.

[0361] Consistent with the breadth-first strategy, this approach involves simplifying assumptions. Rigid protein and small molecule geometry is maintained throughout. As a first approximation rigid geometry is acceptable as the energy minimized coordinates of a deduced structure, describe an energy minimum for the molecule, albeit a local one. If the surface residues of the site of interest are not involved in crystal contacts then the crystal configuration of those residues is used merely as a starting point for energy minimization, and potential solution structures for those residues determined. The deduced structure should reasonably mimic the mean solution configuration.

[0362] A further assumption implicit in CLIX is that the potential ligand, when introduced into the binding pocket or site of a receptor, does not induce change in the protein's stereochemistry or partial charge distribution and so alter the basis on which the GRID interaction energy maps were computed. It must also be stressed that the interaction sites predicted by GRID are used in a positional and type sense only, i.e., when a candidate atomic group is placed at a site predicted as favorable by GRID, no check is made to ensure that the bond geometry, the state of protonation, or the partial charge distribution favors a strong interaction between the protein and that group. Such detailed analysis should form part of more advanced modeling of candidates identified in the CLIX shortlist.

[0363] Yet another embodiment of a computer-assisted molecular design method for identifying ligands of a binding pocket of the invention comprises the de novo synthesis of potential ligands by algorithmic connection of small molecular fragments that will exhibit the desired structural and electrostatic complementarity with an active site or binding pocket of the receptor. The methodology employs a large template set of small molecules with are iteratively pieced together in a model of a binding pocket. Each stage of ligand growth is evaluated according to a molecular mechanics-based energy function, which considers van der Waals and coulombic interactions, internal strain energy of the lengthening ligand, and desolvation of both ligand and receptor. The search space can be managed by use of a data tree that is kept under control by pruning according to the binding criteria.

[0364] In an illustrative embodiment, the search space is limited to consider only amino acids and amino acid analogs as the molecular building blocks. Such a methodology generally employs a large template set of amino acid conformations, though need not be restricted to just the 20 natural amino acids, as it can easily be extended to include other related fragments of interest to the medicinal chemist, e.g. amino acid analogs. The putative ligands that result from this construction method are peptides and peptide-like compounds rather than the small organic molecules that are typically the goal of drug design research. The appeal of the peptide building approach is not that peptides are preferable to organics as potential pharmaceutical agents, but rather that: (1) they can be generated relatively rapidly de novo; (2) their energetics can be studied by well-parameterized force field methods; (3) they are much easier to synthesize than are most organics; and (4) they can be used in a variety of ways, for peptidomimetic ligand design, protein-protein binding studies, and even as shape templates in the more commonly used 3D organic database search approach described above.

[0365] Such a de novo peptide design method has been incorporated in a software package called GROW (Moon et al. (1991) Proteins 11:314-328). In a typical design session, standard interactive graphical modeling methods are employed to define the structural environment in which GROW is to operate. For instance, environment could be an active site binding pocket of an F-box protein, or it could be a set of features on the protein's surface to which the user wishes to bind a peptide-like molecule. The GROW program then operates to generate a set of potential ligand molecules. Interactive modeling methods then come into play again, for examination of the resulting molecules, and for selection of one or more of them for further refinement.

[0366] To illustrate, GROW operates on an atomic coordinate file generated by the user in the interactive modeling session, such as the coordinates provided in Table 4, or the coordinates of a binding pocket or active site as described in Tables 2 and 4 plus a small fragment (e.g., an acetyl group) positioned in the active site to provide a starting point for peptide growth. These are referred to as “site” atoms and “seed” atoms, respectively. A second file provided by the user contains a number of control parameters to guide the peptide growth (Moon et al. (1991) Proteins 11:314-328).

[0367] The operation of the GROW algorithm is conceptually fairly simple. GROW proceeds in an iterative fashion, to systematically attach to the seed fragment each amino acid template in a large preconstructed library of amino acid conformations. When a template has been attached, it is scored for goodness-of-fit to the receptor site or binding pocket, and then the next template in the library is attached to the seed. After all the templates have been tested, only the highest scoring ones are retained for the next level of growth. This procedure is repeated for the second growth level; each library template is attached in turn to each of the bonded seed/amino acid molecules that were retained from the first step, and then scored. Again, only the best of the bonded seed/dipeptide molecules that result are retained for the third level of growth. The growth of peptides can proceed in the N-to-C direction only, the reverse direction only, or in alternating directions, depending on the initial control specifications supplied by the user. Successive growth levels therefore generate peptides that are lengthened by one residue. The procedure terminates when the user-defined peptide length has been reached, at which point the user can select from the constructed peptides those to be studied further. The resulting data provided by the GROW procedure includes not only residue sequences and scores, but also atomic coordinates of the peptides, related directly to the coordinate system of the binding site atoms.

[0368] In yet another embodiment, potential pharmacophoric compounds can be determined using a method based on an energy minimization-quenched molecular dynamics algorithm for determining energetically favorable positions of functional groups in the binding pockets of the invention. The method can aid in the design of molecules that incorporate such functional groups by modification of known ligands or de novo construction.

[0369] For example, the multiple copy simultaneous search method (MCSS) described by Miranker et al. (1991) Proteins 11: 29-34 may be employed. To determine and characterize a local minima of a functional group in the forcefield of the protein, multiple copies of selected functional groups are first distributed in a binding pocket of interest on the F-box protein. Energy minimization of these copies by molecular mechanics or quenched dynamics yields the distinct local minima. The neighborhood of these minima can then be explored by a grid search or by constrained minimization. In one embodiment, the MCSS method uses the classical time dependent Hartee (TDH) approximation to simultaneously minimize or quench many identical groups in the forcefield of the protein.

[0370] Implementation of the MCSS algorithm requires a choice of functional groups and a molecular mechanics model for each of them. Groups must be simple enough to be easily characterized and manipulated (3-6 atoms, few or no dihedral degrees of freedom), yet complex enough to approximate the steric and electrostatic interactions that the functional group would have in binding to the pocket or site of interest in the F-box protein. A preferred set is, for example, one in which most organic molecules can be described as a collection of such groups (Patai's Guide to the Chemistry of Functional Groups, ed. S. Patai (New York: John Wiley, and Sons, (1989)). This includes fragments such as acetonitrile, methanol, acetate, methyl ammonium, dimethyl ether, methane, and acetaldehyde.

[0371] Determination of the local energy minima in the binding pocket or site requires that many starting positions be sampled. This can be achieved by distributing, for example, 1,000-5,000 groups at random inside a sphere centered on the binding site; only the space not occupied by the protein needs to be considered. If the interaction energy of a particular group at a certain location with the protein is more positive than a given cut-off (e.g. 5.0 kcal/mole) the group is discarded from that site. Given the set of starting positions, all the fragments are minimized simultaneously by use of the TDH approximation (Elber et al. (1990) J Am Chem Soc 112: 9161-9175). In this method, the forces on each fragment consist of its internal forces and those due to the protein. The essential element of this method is that the interactions between the fragments are omitted and the forces on the protein are normalized to those due to a single fragment. In this way simultaneous minimization or dynamics of any number of functional groups in the field of a single protein can be performed.

[0372] Minimization is performed successively on subsets of, for example 100, of the randomly placed groups. After a certain number of step intervals, such as 1,000 intervals, the results can be examined to eliminate groups converging to the same minimum. This process is repeated until minimization is complete (e.g. RMS gradient of 0.01 kcal/mole/C). Thus the resulting energy minimized set of molecules comprises what amounts to a set of disconnected fragments in three dimensions representing potential pharmacophores.

[0373] The next step then is to connect the pharmacophoric pieces with spacers assembled from small chemical entities (atoms, chains, or ring moieties). In a preferred embodiment, each of the disconnected can be linked in space to generate a single molecule using such computer programs as, for example, NEWLEAD (Tschinke et al. (1993) J Med Chem 36: 3863,3870). The procedure adopted by NEWLEAD executes the following sequence of commands: (1) connect two isolated moieties, (2) retain the intermediate solutions for further processing, (3) repeat the above steps for each of the intermediate solutions until no disconnected units are found, and (4) output the final solutions, each of which is a single molecule. Such a program can use for example, three types of spacers: library spacers, single-atom spacers, and fuse-ring spacers. The library spacers are optimized structures of small molecules such as ethylene, benzene and methylamide. The output produced by programs such as NEWLEAD consist of a set of molecules containing the original fragments now connected by spacers. The atoms belonging to the input fragments maintain their original orientations in space. The molecules are chemically plausible because of the simple makeup of the spacers and functional groups, and energetically acceptable because of the rejection of solutions with van-der Waals radii violations.

[0374] Compounds and entities (e.g. ligands) of F-box proteins, in particular cdc4 proteins, or SCF complexes identified using the above-described methods may be prepared using methods described in standard reference sources utilized by those skilled in the art. For example, organic compounds may be prepared by organic synthetic methods described in references such as March, 1994, Advanced Organic Chemistry: Reactions, Mechanisms, and Structure, New York, McGraw Hill.

[0375] Test compounds and ligands which are identified using a crystal or model of the present invention can be screened in assays such as those well known in the art. Screening may be for example in vitro, in cell culture, and/or in vivo. Biological screening assays preferably centre on activity-based response models, binding assays (which measure how well a compound binds to a binding pocket of a receptor), and bacterial, yeast, and animal cell lines (which measure the biological effect of a compound in a cell). The assays may be automated for high throughput screening in which large numbers of compounds can be tested to identify compounds with the desired activity. The biological assay may also be an assay for the binding activity of a compound that selectively binds to the binding pocket compared to other receptors.

[0376] Ligands/Compounds Identified by Screening Methods

[0377] The present invention provides a ligand or compound identified by a screening method of the present invention. A ligand or compound may have been designed rationally by using a model according to the present invention. A ligand or compound identified using the screening methods of the invention may specifically associate with a target compound, or part thereof (e.g. a binding pocket). In the present invention the target compound may be the F-box protein or SCF complex or part thereof, or a molecule that is capable of associating with an F-box protein or SCF complex or part thereof (for example a substrate).

[0378] A ligand or compound identified using a screening method of the invention may act as a “modulator”, i.e. a compound which affects the activity of an F-box protein or SCF complex. A modulator may reduce, enhance or alter the biological function of an F-box protein or an SCF E3 ubiquitin ligase. For example a modulator may modulate the capacity of the F-box protein or an SCF E3 ubiquitin ligase to interact with its substrate. An alteration in biological function may be characterised by a change in specificity. For example, a modulator may cause the F-box protein to interact with a different substrate. In order to exert its function, the modulator commonly binds to a binding pocket.

[0379] A “modulator” which is capable of reducing the biological function of the enzyme may also be known as an inhibitor. Preferably an inhibitor reduces or blocks the capacity of the F-box protein or an SCF E3 ubiquitin ligase to interact with its substrate thus reducing or blocking ubiquitination of the substrate. The inhibitor may mimic the binding of a substrate, for example, it may be a substrate analogue. A substrate analogue may be designed by considering the interactions between the substrate and the F-box protein or an SCF E3 ubiquitin ligase (for example, by using information derivable from the crystal of the invention) and specifically altering one or more groups (as described above).

[0380] The present invention also provides a method for modulating the activity of an F-box protein, in particular a cdc4 protein, using a modulator according to the present invention. The invention also provides a method for modulating (e.g. potentiating or inhibiting) ubiquitination of a substrate by an SCF E3 ubiquitin ligase, by potentiating or inhibiting the substrate binding pocket of the ligase. Inhibition of ubiquitination of a substrate may decrease signaling and inhibit cellular processes that may be involved in disease. It would be possible to monitor cellular processes following such treatments by a number of methods known in the art.

[0381] A modulator may be an agonist, partial agonist, partial inverse agonist or antagonist of an F-box protein.

[0382] As mentioned above, a substrate or an identified ligand may act as a ligand model (for example, a template) for the development of other compounds. A modulator may be a mimetic of a substrate or ligand.

[0383] Like the test compound (see above) a modulator may be one or a variety of different sorts of molecule. (See examples herein.) A modulator may be an endogenous physiological compound, or it may be a natural or synthetic compound. The term “modulator” also refers to a chemically modified ligand or substrate.

[0384] The technique suitable for preparing a modulator will depend on its chemical nature. For example, peptides can be synthesized by solid phase techniques (Roberge J Y et al (1995) Science 269: 202-204) and automated synthesis may be achieved, for example, using the ABI 43 1 A Peptide Synthesizer (Perkin Elmer) in accordance with the instructions provided by the manufacturer. Once cleaved from the resin, the peptide may be purified by preparative high performance liquid chromatography (e.g., Creighton (1983) Proteins Structures and Molecular Principles, WH Freeman and Co, New York N.Y.). The composition of the synthetic peptides may be confirmed by amino acid analysis or sequencing (e.g., the Edman degradation procedure; Creighton, supra).

[0385] If a modulator is a nucleotide, or a polypeptide expressable therefrom, it may be synthesized, in whole or in part, using chemical methods well known in the art (see Caruthers M H et al (1980) Nuc Acids Res Symp Ser 215-23, Horn T et al (1980) Nuc Acids Res Symp Ser 225-232), or it may be prepared using recombinant techniques well known in the art.

[0386] Organic compounds may be prepared by organic synthetic methods described in references such as March, 1994, Advanced Organic Chemistry: Reactions, Mechanisms, and Structure, New York, McGraw Hill.

[0387] The invention also relates to classes of modulators of F-box proteins, in particular cdc4 proteins based on the structure and shape of a substrate or component thereof, defined in relation to the substrate's spatial association with a crystal structure of the invention or part thereof.

[0388] A class of modulators may comprise a compound containing a structure of a CPD motif. In particular, the modulators can comprise a CPD motif having the structural coordinates of the CPD motif in the active site binding pocket of an F-box protein. In an embodiment, a modulator comprises the structural coordinates of a CPD motif having the structural coordinates listed in Table 6.

[0389] The invention contemplates all optical isomers and racemic forms of the modulators of the invention.

[0390] Pharmaceutical Composition

[0391] The present invention also provides for the use of a modulator according to the invention, in the manufacture of a medicament to treat and/or prevent a disease in a mammalian patient. There is also provided a pharmaceutical composition comprising such a modulator and a method of treating and/or preventing a disease comprising the step of administering such a modulator or pharmaceutical composition to a subject, preferably a mammalian patient.

[0392] The pharmaceutical compositions may be for human or animal usage in human and veterinary medicine and will typically comprise a pharmaceutically acceptable carrier, diluent, excipient, adjuvant or combination thereof.

[0393] Acceptable carriers or diluents for therapeutic use are well known in the pharmaceutical art, and are described, for example, in Remington's Pharmaceutical Sciences, Mack Publishing Co. (A. R. Gennaro edit. 1985). The choice of pharmaceutical carrier, excipient or diluent can be selected with regard to the intended route of administration and standard pharmaceutical practice. The pharmaceutical compositions may comprise as—or in addition to—the carrier, excipient or diluent any suitable binder(s), lubricant(s), suspending agent(s), coating agent(s), solubilising agent(s).

[0394] Preservatives, stabilizers, dyes and even flavouring agents may be provided in the pharmaceutical composition. Examples of preservatives include sodium benzoate, sorbic acid and esters of p-hydroxybenzoic acid. Antioxidants and suspending agents may also be used.

[0395] The routes for administration (delivery) include, but are not limited to, one or more of: oral (e.g. as a tablet, capsule, or as an ingestable solution), topical, mucosal (e.g. as a nasal spray or aerosol for inhalation), nasal, parenteral (e.g. by an injectable form), gastrointestinal, intraspinal, intraperitoneal, intramuscular, intravenous, intrauterine, intraocular, intradermal, intracranial, intratracheal, intravaginal, intracerebroventricular, intracerebral, subcutaneous, ophthalmic (including intravitreal or intracameral), transdermal, rectal, buccal, vaginal, epidural, sublingual.

[0396] Where the pharmaceutical composition is to be delivered mucosally through the gastrointestinal mucosa, it should be able to remain stable during transit though the gastrointestinal tract; for example, it should be resistant to proteolytic degradation, stable at acid pH and resistant to the detergent effects of bile.

[0397] Where appropriate, the pharmaceutical compositions can be administered by inhalation, in the form of a suppository or pessary, topically in the form of a lotion, gel, hydrogel, solution, cream, ointment or dusting powder, by use of a skin patch, orally in the form of tablets containing excipients such as starch or lactose or chalk, or in capsules or ovules either alone or in admixture with excipients, or in the form of elixirs, solutions or suspensions containing flavouring or colouring agents, or they can be injected parenterally, for example intravenously, intramuscularly or subcutaneously. For parenteral administration, the compositions may be best used in the form of a sterile aqueous solution which may contain other substances, for example enough salts or monosaccharides to make the solution isotonic with blood. The aqueous solutions should be suitably buffered (preferably to a pH of from 3 to 9), if necessary. The preparation of suitable parenteral formulations under sterile conditions is readily accomplished by standard pharmaceutical techniques well-known to those skilled in the art.

[0398] If the agent of the present invention is administered parenterally, then examples of such administration include one or more of: intravenously, intra-arterially, intraperitoneally, intrathecally, intraventricularly, intraurethrally, intrasternally, intracranially, intramuscularly or subcutaneously administering the agent; and/or by using infusion techniques.

[0399] For buccal or sublingual administration the compositions may be administered in the form of tablets or lozenges which can be formulated in a conventional manner.

[0400] The tablets may contain excipients such as microcrystalline cellulose, lactose, sodium citrate, calcium carbonate, dibasic calcium phosphate and glycine, disintegrants such as starch (preferably corn, potato or tapioca starch), sodium starch glycollate, croscarmellose sodium and certain complex silicates, and granulation binders such as polyvinylpyrrolidone, hydroxypropylmethylcellulose (HPMC), hydroxypropylcellulose (HPC), sucrose, gelatin and acacia. Additionally, lubricating agents such as magnesium stearate, stearic acid, glyceryl behenate and talc may be included.

[0401] Solid compositions of a similar type may also be employed as fillers in gelatin capsules. Preferred excipients in this regard include lactose, starch, cellulose, milk sugar or high molecular weight polyethylene glycols. For aqueous suspensions and/or elixirs, the agent may be combined with various sweetening or flavouring agents, colouring matter or dyes, with emulsifying and/or suspending agents and with diluents such as water, ethanol, propylene glycol and glycerin, and combinations thereof.

[0402] As indicated, a therapeutic agent (e.g. modulator) of the present invention can be administered intranasally or by inhalation and is conveniently delivered in the form of a dry powder inhaler or an aerosol spray presentation from a pressurised container, pump, spray or nebuliser with the use of a suitable propellant, e.g. dichlorodifluoromethane, trichlorofluoromethane, dichlorotetrafluoroethane, a hydrofluoroalkane such as 1,1,1,2-tetrafluoroethane (HFA 134A™) or 1,1,1,2,3,3,3-heptafluoropropane (HFA 227EA™), carbon dioxide or other suitable gas. In the case of a pressurised aerosol, the dosage unit may be determined by providing a valve to deliver a metered amount. The pressurised container, pump, spray or nebuliser may contain a solution or suspension of the active compound, e.g. using a mixture of ethanol and the propellant as the solvent, which may additionally contain a lubricant, e.g. sorbitan trioleate. Capsules and cartridges (made, for example, from gelatin) for use in an inhaler or insufflator may be formulated to contain a powder mix of the agent and a suitable powder base such as lactose or starch.

[0403] Therapeutic administration of polypeptide modulators may also be accomplished using gene therapy. A nucleic acid including a promoter operatively linked to a heterologous polypeptide may be used to produce high-level expression of the polypeptide in cells transfected with the nucleic acid. DNA or isolated nucleic acids may be introduced into cells of a subject by conventional nucleic acid delivery systems. Suitable delivery systems include liposomes, naked DNA, and receptor-mediated delivery systems, and viral vectors such as retroviruses, herpes viruses, and adenoviruses.

[0404] Applications

[0405] The invention further provides a method of treating a mammal, the method comprising administering to a mammal a modulator or pharmaceutical composition of the present invention.

[0406] In particular, the invention contemplates a method of treating or preventing a condition or disease associated with an F-box protein or SCF complex in a cellular organism, comprising:

[0407] (a) administering a modulator of the invention in an acceptable pharmaceutical preparation; and

[0408] (b) activating or inhibiting an F-box protein or SCF complex or their interaction with a substrate to treat or prevent the disease.

[0409] The invention provides for the use of a modulator identified by the methods of the invention in the preparation of a medicament to treat or prevent a disease in a cellular organism. Use of modulators of the invention to manufacture a medicament is also provided.

[0410] Typically, a physician will determine the actual dosage of a modulator or pharmaceutical composition of the invention that will be most suitable for an individual subject and it will vary with the age, weight and response of the particular patient and severity of the condition. There can, of course, be individual instances where higher or lower dosage ranges are merited.

[0411] The specific dose level and frequency of dosage for any particular patient may be varied and will depend upon a variety of factors including the activity of the specific compound employed, the metabolic stability and length of action of that compound, the age, body weight, general health, sex, diet, mode and time of administration, rate of excretion, drug combination, the severity of the particular condition, and the individual undergoing therapy. By way of example, the pharmaceutical composition of the present invention may be administered in accordance with a regimen of 1 to 10 times per day, such as once or twice per day.

[0412] For oral and parenteral administration to human patients, the daily dosage level of the agent may be in single or divided doses.

[0413] The modulators and compositions of the invention may be useful in the prevention and treatment of conditions involving aberrant F-box proteins or SCF complexes. In particular the modulators and compositions may be useful in treating cancer or Alzheimer's Disease.

[0414] Conditions which may be prevented or treated in accordance with the invention include but are not limited to lymphoproliferative conditions, and malignant and pre-malignant conditions. Malignant and pre-malignant conditions may include solid tumors, B cell lymphomas, chronic lymphocytic leukemia, chronic myelogenous leukemia, prostate hypertrophy, Hirschsprung disease, glioblastoma, breast and ovarian cancer, adenocarcinoma of the salivary gland, premyelocytic leukemia, prostate cancer, multiple endocrine neoplasia type IIA and IIB, medullary thyroid carcinoma, papillary carcinoma, papillary renal carcinoma, hepatocellular carcinoma, gastrointestinal stromal tumors, sporadic mastocytosis, acute myeloid leukemia, large cell lymphoma or Alk lymphoma, chronic myeloid leukemia, hematological/solid tumors, papillary thyroid carcinoma, stem cell leukemia/lymphoma syndrome, acute myelogenous leukemia, osteosarcoma, multiple myeloma, preneoplastic liver foci, and resistance to chemotherapy.

[0415] Modulators and compositions of the invention may be used to restore function to a mutant F-box protein, in particular a mutant cdc4 polypeptide. Modulators and compositions of the invention, in particular inhibitors may also have utility in treating diseases associated with F-box mutations, in particular cdc4 polypeptide mutations, in combination with other cancer mutations, Notch pathway mutations or presenilin mutations.

[0416] A modulator of the invention may be used to promote binding of a substrate to a SCF complex. In an embodiment a modulator that associates (preferably with high affinity) with a binding pocket of a SCF complex as described herein, is linked to an agent that binds to a substrate to be ubiquitinated by a SCF complex. A modulator-agent-substrate complex where the modulator is derived from a binding pocket of an F-box protein as described herein may be used in treating diseases associated with a mutant F-box protein.

[0417] Therapeutic efficacy and toxicity of compositions and modulators of the invention may be determined by standard pharmaceutical procedures in cell cultures or with experimental animals, such as by calculating the ED₅₀ (the dose therapeutically effective in 50% of the population) or LD₅₀ (the dose lethal to 50% of the population) statistics. The therapeutic index is the dose ratio of therapeutic to toxic effects and it can be expressed as the ED₅₀/LD₅₀ ratio. Pharmaceutical compositions that exhibit large therapeutic indices are preferred.

[0418] The invention will now be illustrated by the following non-limiting examples:

EXAMPLE 1

[0419] The following methods were used in the investigation described in the example:

[0420] Methods

[0421] Cloning, Protein Expression and Purification

[0422] The Cdc4 fragment employed for crystalization, which is deleted for terminal residues 1 to 262 and 745 to 779, extends from the beginning of the F-box domain to the end of the WD40 repeat domain. The N-terminal deletion removes a poorly conserved sequence of 226 amino acids and a conserved element of approximately 40 residues termed the D-domain that immediately precedes the fbox domain and that has been implicated in molecular multimerization. The C terminal deletion removes residues not conserved amongst different Cdc4 homologues. Both Skp1 and Cdc4 were engineered to remove flexible loops, namely residues 36-55 in Skp1 and residues 601 to 604 and 609 to 624 in Cdc4.

[0423] A PCR product containing CDC4(263-744) was cloned into the EheI(SfoI) and BamH1 sites of pPROEX HTb. In parallel, a PCR product containing SKP1Δ37-64 was cloned into the NdeI and BamHI sites of pGEX2T-TEV. An SspI GST-SKP1-containing fragment from this construct was cloned into the StuI site of the Cdc4 construct described above such that CDC4 and SKP1 were in opposite orientations. A non-homologous region in CDC4 encoding amino acids 602-624 was then replaced by the DNA sequence GGCGAACTG [SEQ ID NO. 39], which encodes the shorter peptide sequence Gly-Glu-Leu.

[0424] The Cdc4/skp1 complex was expressed in E. coli B934 (DE3) cells grown in minimal media suplemented with a mixture of selenomethionine (40 ug/ml) and methionine (0.4 ug/ml). Cells were induced with 0.2 mM isopropyl-β-D-thiogalactopyranoside (IPTG) at 15° C. overnight. Cell pellets were resuspended in 50 mM hepes pH 7.5, 500 mM NaCl, 10% glycerol, and 5 mM Imidazole, lysed with a cell homogenizer (Emulsiflex C-5, Avistin) followed by a 20 sec sonication (vibra cell, Betatec). The lysate was then clarified by centrifugation at 65 000×g for 40 min. The supernatant was loaded onto a 5 ml metal chelating column (Pharmacia) and eluted in high imidazole. This fraction was loaded onto a glutathione-sepharose column (Pharmacia) and the bound complex was eluted by overnight digestion with TEV protease (Canadian Life). Eluted protein was dialysed to remove DTT and EDTA and reloaded onto a metal chelating column. The flow through containing the complex was concentrated and applied to a Superdex S 75 gel filtration column (Pharmacia). Fractions containing the complex were concentrated in a buffer containing 10 mM hepes pH 7.5, 250 mM NaCl, and 1 m M DTT.

[0425] Crystallization, Data Collection, and Structure Determination

[0426] Hanging drops containing 1 μl of 21 mg/ml protein plus 1.2 molar equivilents of the CPD peptide sequence were mixed with equal volumes of reservoir buffer containing 0.1 M Tris pH 8.5, and 1.5 M ammonium sulphate. Crystals were flash frozen in reservoir buffer supplemented with 15% glycerol. Crystals of the space group P3₂, (α=107.7 Å, b=107.7 Å, c=168.3 Å, α=γ=90°, β=120°), with two molecules of the complex in the asymmetric unit were obtained at 20° C. A Multiple Anomalous Dispersion (MAD) experiment was performed on a frozen crystal at the Advanced Photon Source (Argonne, Ill.) (APS) beamline BM 14-B and BM 14-D(λ1=0.9798 Å, λ2=0.9800 Å, λ3=0.9000 Å) using a Quantum 4 ADSC CCD detector. Data processing and reduction was carried out with the HKL program suite (Otwinowski and Minor, 1997). The programs SHARP (de La Fortelle and Bricogne, 1997) and SnB (Miller et al., 1994) were used in combination to locate and refine 19 of the 22 Se sites. Following density modification with Solomon (Abrahams and Leslie, 1996), a partial model was generated using 0 (Jones et al., 1991) and refined using CNS (Brunger et al., 1998) to a working R value of 24.09% and a free R value of 28.71%. Pertinent statistics for data collection and refinement are shown in Table 1.

[0427] The increased order of the second CPDs may be due to a crystal packing interaction involving the c-terminus of the CPD. While the main chain termini of the second CPD are discernable (FIG. 3e), the precise backbone and side chain conformations for the P−2 Leu, P−3 Gly, P+4 Ser, and P+5 Gly are less reliably determined.

[0428] Mutagenesis

[0429] Point mutants were obtained by a PCR-based approach using oligos provided in supplementary information and Pfu polymerase (Stratagene). Once verified by sequencing the mutants were sub-cloned into the appropriate vectors as listed in the supplementary information. Alanine insertion mutations were obtained using the Kunkel method (ref) and then sub-cloned into the vectors indicated in the supplementary information.

[0430] Shuffle Experiments

[0431] All mutants on a TRP1 ARS CEN plasmid were transformed into a cdc4Δ strain (MT 1259) containing a wildtype copy of CDC4 on a URA3 ARS CEN plasmid. Cells were plated on either Trp⁻Ura⁻ or 5-FOA medium for 2 days at 30° C. Viable cells on 5-FOA were grown in Trp medium and transformed with either wild type GAL1-SIC1, GAL1-SIC T45A, or GAL1-SIC T33V on a LEU2 ARS CEN pasmid. Cells were then plated on Leu- Trp-plates containing either glucose or galactose and incubated for 2 days at 30° C.

[0432] Sic1-Cdc4 Interactions.

[0433] Bacterially expressed His6-Sic1 was phosphorylated with Cln2-Cdc28 kinase purified from baculovirus infected Sf9 cells as described before (Nature paper). 1 ug of WT or mutant Cdc4-GST-Skp1, immoblized on GSH-Sepharose resin, was incubated with 0.5 ug phospho-Sic1 at 4 C for 1 h and washed 4 times. Captured complexes were resolved on SDS-PAGE and Sic1 visualized by anti-Sic1 Western blotting and ECL. For IEF-2D analysis, several Sic1 phosphorylation reactions were carried out for different time periods to obtain a spectrum of Sic1 that were phosphorylated at different numbers of its nine CDK sites. This pool of phospho-Sic1 (2.5 ug) was incubated with 5 μg of WT or mutant Cdc4-GST-Skp1 as described above. Different phosphorylation states of Sic1 were separated by denaturing isoelectric focusing (IEF)-2D gel electrophoresis and visualized by anti-Sic1 Western blotting and ECL. IEF was performed using pH 3-10NL Immobiline gel strips and IPGphore IEF system (Amersham pharmacia).

[0434] Results

[0435] The x-ray crystal structure presented herein consists of a ternary complex of yeast Skp1 bound to a fragment of Cdc4, and a 9mer high affinity CPD phosphopeptide (FIG. 2). The Cdc4 fragment, which is deleted for terminal residues 1 to 262 and 745 to 779, extends from the beginning of the F-box domain to the end of the WD40 repeat domain.

[0436] Skp1-Cdc4 Fbox: Skp1 forms an elongated structure with a mixed α/β topology identical to that reported for human Skp1 (Schulman et al, 2000). The topology consists of a three-strand (denoted β1 to β3) β-sheet and eight α-helices, denoted α1 to α8 (FIG. 2a). The structure of Cdc4 from its amino terminus consists of an F-box domain, an α-helical extension or linker, and a WD40 repeat domain (FIG. 2a,b). The F-box domain comprises five a helices (denoted α0 to α4){tilde over (.)} This topology differs slightly from that reported for the F-box domain of hSkp2 (Schulman et al, 2000), which consists of a loop region L1 and three helices denoted α1 to α3. Helix α0 in Cdc4 corresponds most closely in sequence and position to the loop region L1 of Skp2 while a half turn remnant of helix α4 is discernable in the transition sequence between the Skp2 F-box and Leucine Repeat domains. As observed in the Skp1-Skp2 complex, Skp1 and the F-box domain of Cdc4 associate by the interdigiation of helixes α0 to α3 of Cdc4 with helices α5 to α8 of Skp1. This mode of inter-domain association is characterized by a common and continuous hydrophobic core that spans the two protein domains.

[0437] Cdc4 helical linker and WD40 domain: Following the F-box domain of Cdc4 is a helical extension that forms a structured bridge to the WD40 repeat domain. The helical extension consists of two α-helices α5 and α6 that together with helices α3 and α4 of the F-box domain form a stalk and pedestal like structure that connects and orients the WD40 domain (FIG. 2c).

[0438] Eight copies of the WD40 repeat motif in Cdc4 form an 8 blade β-propeller structure. Each blade, composed of 4 anti-parallel β-strands, is related by 8-fold pseudo symmetry about a central axis (FIG. 2b). As first shown for G-protein gamma subunit (Sondek 1996), the WD40 repeat motif of approximately 40 amino acids composes the outer β-strand of one propeller blade and the inner three strands of the adjacent blade. A continuous circular arrangement of blades is formed by the association of the first and last WD40 repeat motifs to form the 8^(th) propeller blade. Interestingly, a 7 β-propeller blade structure was anticipated for Cdc4 and its orthologues (and generally all WD40 repeat F-box adaptors), which is attributable in part to the cryptic nature of the 8th WD40 repeat motif (FIG. 1). Based on the structure based sequence alignment in FIG. 1, it is predicted that the other WD40 class of F-box adaptor proteins (i.e. the Met30 orthologues and βTRCP orthologues) will form 7-blade β-propeller structures.

[0439] The WD40 repeat domain forms a disk like structure characterized by a cavity in the middle and two opposing circular surfaces of slightly different size. The smaller of the two surfaces composes the CPD binding site. On the bottom surface is anchored helix α6 of the helical extension, which inserts obliquely between propeller blades β7 and β8. Interestingly, β-propeller blade 2 consists of 5 β-strands. The outermost strand of this blade, denoted β9¹, is non-standard and arises from an amino acid insert in the connecting loop between α-strands 12 and 13. Strand β9¹, forms a parallel arrangement with strand β9, which differs from the anti parallel architecture of all other 1-strand elements in the WD40 domain structure. A large insert in the β12-β13 linker is absent from dr, ce, hu, mu Cdc4 homologues suggesting that a 5 {tilde over (β)} strand propeller blade 2 is unique to the fungal homologues.

[0440] A fixed orientation between the F-box domain and WD40 domain of Cdc4 is maintained largely through the integrity of the stalk like helix α6 of the helical extension (FIG. 2c). Helix α6 is 30 Å in length, and is anchored at its N-terminus to the hydrophobic core of the F-box/helical extension and at its C-terminus to the hydrophobic core of the WD40 repeat domain. In contrast to the intermolecular connection between Skp1 and the F-box domain, the connection between the F-box domain and WD40 repeat domain appears less rigidly structured.

[0441] At its amino terminus, helix α6 anchors to the F-box through hydrophobic interactions involving α6 residues Phe 355 and Leu 356 and F-box residues Ile 295, and Ile 296, Leu 315, Trp 316, and Leu 319 (FIG. 2c). Helix α5 packs along side the base of helix α6 opposite to the F-box domain through hydrophobic packing interactions involving Tyr342, Leu 338 and Leu 334. At its C-terminus, helix α6 anchors through hydrophobic interactions involving residues Trp 365 and Ile 364 with WD repeat residues Val 687, Ile 696, Leu 726 and Phe 743 in β-propeller blades 7 and 8. Asn 364 of helix α6 also forms a tight hydrogen bond interaction with the backbone carbonyl group of Phe 743 in propeller blade 8. The noted interactions (with the exception of interactions involving helix α5) involve residues that are conserved across most WD40 F-box adaptor proteins including the Met30 orthologues and β-TRCP orthologues, which suggests that the linkage between WD40 and F-box domains are similarly structured in these proteins. Helix α6 in β-TRCP, however, appears to be one α-helical turn longer (FIG. 1).

[0442] Outside of stalk helix α6, only two close contacts (<3.5 Å) are observed between the WD40 repeat domain and other regions of Cdc4. These contacts consist of hydrogen bonds between Asn684 and Arg700 in the loop regions of propeller blade 7 with Glu 323 in the α4-α5 linker of the helical extension. Both, hydrogen bonds are maintained in the two Cdc4 molecules of the crystal asymmetric unit but all three residues are poorly conserved amongst Cdc4 orthologues (FIG. 1). The lack of additional stabilizing interactions suggests that the F-box/WD40 domain linkage is not exceedingly rigid, and indeed, the WD40 domain in the two molecules of the asymmetric unit differ relative to their F-box domains by a 5 degree rotation about helix α6.

[0443] WD40 domain phosphopeptide recognition: A nine-mer CPD consisting of the sequence acetyl-Gly,Leu,Leu,pThr,Pro,Pro,Gln,Ser,Gly-amide [SEQ ID NO.40] is bound to the front face of the WD40 domain of Cdc4. In the two WD40 repeat domain/CPD complexes of the crystal asymmetric unit, a central core of 4 CPD residues corresponding to the sequence Leu, pThr, Pro, Pro [SEQ ID NO.41] is well ordered.

[0444] These residues have been modeled unambiguously in unbiased experimental electron density maps (FIG. 3e). Interpretable electron density is also apparent for the P−2 Leu, P−3 Gly, P+3 Gln, P+4 Ser, and P+5Gly positions of the second CPD (no interpretable electron density is apparent for these residues in the first CPD). The CPD binds in an extended manner across β-propeller blade 2 with the N-terminus oriented towards the central cavity of the WD40 repeat domain and the C-terminus oriented towards the outer rim. The CPD binding surface of Cdc4 is composed of invariant and highly conserved residues from β-propeller blades 1 to 6 and 8 and represents the most conserved part of the WD40 repeat domain surface (FIG. 3a,c).

[0445] Cdc4 displays an absolute requirement for phosphorylation at Ser or Thr at the P−0 position of the CPD. In the crystal structure, the P0 pThr phosphate group is coordinated by an intricate network of electrostatic interactions and hydrogen bonds involving residues absolutely conserved across all Cdc4 orthologues (FIG. 3c). The P0 phosphate group forms direct electrostatic interactions with the guanidinium groups of Arg 485, Arg 467, and Arg 534 and a direct hydrogen bond with the side chain of Tyr 548. The side chain of Tyr 548 is coordinated by stacking interactions with the guanidinium group of Arg 572, which in turn is coordinated by a hydrogen bond to the side chain of Tyr 574. Although Cdc4 shows a strong (6 fold) preference for pThr over pSer, the structural basis for this selectivity is not obvious. In the crystal structure, the Cy methyl group of Thr is directed towards solvent and does not make contact with the CPD binding surface of Cdc4. This binding preference may be due to the greater side chain rotational stability arising from the Thr β-branch structure.

[0446] Cdc4 displays an absolute requirement for proline in the p+1 CPD position. In the crystal structure, the P+1 proline side chain projects into a three-sided pocket on the CPD binding surface. The side chain of Trp 426 forms one side of the pocket and packs in a coplanar manner with the P+1 proline side chain. On its other side, the Trp 426 side chain packs tightly against the side chain of Thr 386. The opposite side of the P+1 binding pocket is formed by the side chain of Arg 485. Arg 485 coordinates the P+1 Proline through van der Wals side chain interactions and through a direct hydrogen bond to the Proline backbone carbonyl group. This represents the sole direct hydrogen bond interaction between Cdc4 and the CPD main chain. The side chains of Thr 441 and Thr 465 define the remaining side of the P+1 Proline binding pocket, with the Cy side chain groups composing a hydrophobic surface. The hydroxyl groups of Thr 441 and 465 orient away from the P+1 binding pocket, where they are well placed to influence binding specificity for CPD residues C-terminal to the P+1 position. Unlike Trp 426, Thr 386 and Arg 485, which are invariant amongst the Cdc4 orthologues, Thr 441 and Thr 465 are substituted with Ile in the S. pombe Cdc4 orthologue Pop1. The modeling studies suggest that this substitution has no effect on the P+1 binding pocket but may perturb CPD binding specificity C-terminal to the P+1 positions through steric effects (Ile is bigger than Thr) and by increasing the hydrophobic character of the surface.

[0447] Cdc4 displays a strong preference for the hydrophobic residues Leu, Ile and Proline at the P−1 and P−2 CPD positions. In the crystal structure, the P−1 Leucine side-chain is oriented towards a hydrophobic pocket composed of invariant residues Trp 426, Trp 717, and Thr 386, and the conserved hydrophobic residue Val 384. While less precisely modeled, the main chain position of Leu+2 lies in close proximity to a third hydrophobic pocket composed of the invariant residue Tyr574, and the conserved hydrophobic residues Met 590 and Leu634.

[0448] Cdc4 displays little preference for residues in the P+2 to P+5 CPD positions. In the crystal structure, the side chain of P+2 Pro is directed towards solvent (which would account for the lack of selectivity at this position), while the main chain conformation of Pro+1 and Pro+2, causes the CPD to kink away from the peptide-binding surface from the Pro+2 position onwards. As a result, only one additional close contact with Cdc4 is made by the CPD following the Pro+1 position, which consists of a weak hydrogen bond (sub-optimal geometry) between the P+4 Gln side chain and the side chain of Arg 485.

[0449] Adjacent to the P+1 proline binding pocket, Ser 464, Thr 441 and Thr 465 are well placed to exert specificity for the +3 and +4 CPD positions if an extended rather than kinked conformation of the CPD were adopted. As noted, Thr 441 and 465 are substituted with Ile in the Cdc4 orthologue pop1 in S. pombe. While nothing is known about the effect of this substitution on CPD recognition, it is predicted that this could have some effect on substrate selectivity for the P+2 to P+5 CPD positions.

[0450] Cdc4 displays strong selectivity against Arginine and Lysine in positions −2, −1, +2, +3 and +4. This selectivity may be due to electrostatic repulsion generated by the invariant Cdc4 residues Argininc 572, 534, 467, 485 and 443, which dominate the local electrostatic character of the CPD binding site. Lys 402 is also well placed to contribute to repulsive effects but this position is not conserved amongst the Cdc4 orthologues. The selectivity against positively charged residues in the P−2 to P−1 CPD positions can also be reconciled in part by the hydrophobic nature of the P−1 and P−2 binding pockets and indeed, oppositely charged Glu and Asp residues are also disfavored at these CPD positions.

[0451] Comparison with Skp1-Skp2 Complex:

[0452] Skp2 is a representative member of a second class of F-box adaptor proteins, which possesses a leucine repeat domain in place of the WD40 repeat of Cdc4. In addition to providing a first structural view of a Skp1 homologue and an F-box domain, the structure of the Skp1/Skp2 complex revealed a mode of molecular association predicted to be employed by all Skp1/F-box homologues. The Cdc4/Skp1/CPD structure confirms the fold of the individual Skp1 and F-box domains and their mode of association. Superposition of yeast and h Skp1 strands β1-β3 and helices α1 to α7 (RMSD Cα=0.74 Å) reveals a close correspondence between F-box helixes α1 to α3 with only Skp1 helix α8 and F-box helix α4 showing significant deviations between the two structures. In addition, only the first half of helix α8 is ordered in ySkp1 and only ha half turn fragment of the F-box helix α4 is apparent in Skp2. The differences in positions and lengths of F-box helices α4 and Skp1 helices α8 reflects the different roles these secondary structure elements play in the linkage between their respective F-box and ligand binding domains.

[0453] The structure of the Skp1/Skp2 complex revealed a solid/substantial linkage between its Leucine Repeat and the F-box domains, a feature predicted to be shared by all Skp2 F-box orthologues. In Skp2, the F-box domain helix α4 terminates abruptly and without an appreciable linker, makes an immediate transition to the Leu Repeat domain fold This linkage is enhanced by a β-strand projecting back from C-terminus of the Leu repeat domain and helix α8 projecting forward from Skp1. The sum of linker region interactions compose a local hydrophobic network that links the hydrophobic cores of the F-box domain with that of the LRR domain. This contrast sharply with the corresponding linkage of Cdc4, which is composes primarily by a lengthy inter-domain linker (the helical extension) and which lacks significant involvement of Skp1 or the WD40 repeat domain for stabilization.

[0454] Although the Skp2 and Cdc4 F-box adaptor proteins employ structurally divergent ligand binding domains, the general position of the WD40 and LLR domains are surprisingly similar. The precise ligand-binding site on Skp2 has not been determined but mutagenesis sties on the Skp2 orthologue in Met30 have mapped the ligated binding site to the inner side of the curved surface. If the Skp2 binding site is inferred from the overlap with the Cdc4 CPD binding site, the CPD site would map to the lateral side of the Leu repeat domain.

[0455] Model of the SCF^(Cdc4) E2 Complex

[0456] The structure of Cdc4 bound to substrate provides a missing piece of the larger SCF structural puzzle and sheds light on how substrate is presented for ubiqutination. A complete model of the SCF^(Cdc4)-E2-substrate complex consisting of an E2, a cullin, a ring finger domain, an F-box adaptor, Skp1, and CPD has been constructed using the structures of individual component proteins and/or larger assemblies determined previously (FIG. 4). Two interesting features are apparent. Firstly, a separation distance between the E2 active site cysteine and the peptide-binding site of Cdc4 is very large at 64 Å and second Cdc4 presents the CPD peptide with a direct line of sight to the E2.

[0457] Mutational Analysis of CPD Binding Surface

[0458] In order to probe the functional importance of amino acid residues on the highly conserved peptide binding surface, a panel of Cdc4 mutants (both single and double mutant) were generated and tested each for its ability to bind phospho Sic1 and Skp1 in vitro using a pull down assay and for its ability to substitute for wt-cdc4 in vivo using a cell viability assay. Of 12 single site mutants tested, only Arg 467. Arg485Ala Arg534Ala, and Trp 426 abolished both cell viability in vivo and phosphoSic1 binding in vitro. Together, these residues compose most of the interaction surface with the pThr, Pro CPD core. Interestingly, Tyr 548, the only other amino acid on the surface of CDC4 to directly contact P0 phosphate group, is fractional in vivo but is compromised for CPD binding in vitro. Mutation of the adjacent residue Arg572 to Ala shows the same behavior. For the Arg572 mutation, the inablity to bind psic1 in vitro appears due to its tendency to aggregation. Presumably in the context of the full SCF complex in vivo this mutant is sufficiently well behaved to bind phospho Sic1.

[0459] All other single site mutants including Arg443Ala, Lys402Ala, Tyr574Ala, Trp717, Val384, and the double site mutant Thr441/465IIe, K404D/R443D and V384N/W717N are viable when expressed in the cdc4 delete and are fully competent for phosphoSic1 binding in vitro.

[0460] Since the cell viability assay nay be masking subtle functional roles for the conserved Cdc4 residues, function was assayed in vivo under more stringent conditions in which Sic1 wt or the stabilized mutants, Sic1 (T33V) or Sic1(T45A) are over-expressed under a galactose promoter. This should amplify defects in cdc4 function. Under these conditions, Trp 717, Tyr 548 and the double mutant K404D/R443D are lethal showing that these residues are in fact important for functions

[0461] Role of the Stem and Pedestal Structure

[0462] To probe the role of the F-box WD40 inter-domain linker, point mutations, insertions or deletions were introduced into the stem and pedestal structure of Cdc4 and protein function was assessed as performed for the peptide binding site mutants.

[0463] Deletion of helix α5 or introduction of Proline and Glycine helix destabilizing residues within the helix had no effect n Cdc4 function both in vitro and in vivo. This result is consistent with the poorly conserved nature f helix α5 and its flanking linker regions. Helix 5 appears entirely absent from human, mouse and drosophila homologues and helix destabilizing substitutions in helix 5 incorporating glycine and proline, are observed in the worm and fungal homologues (FIG. 1). A more invasive deletion of helix 5 that deletes part of the linkers to helix 4 and helix 6 was inviable in yeast. This mutant is properly folded as evidence by the finding that the protein can bind both Skp1 and phospho Sic 1 in vitro. This mutation should likely disrupt the positioning of helix 6 relative to the fbox domain (the linker is too short to span the two secondary structure elements).

[0464] The introduction of helix destabilizing residues in helix α6 or the lengthening of the helix by the insertion of one, two, three, four, 8 or 12 amino acid residues also disrupted protein function in vivo, without while maintaining the ability of Cdc4 to to bind pSic1 and Skp1. These results are consistent with a possible role for helix 6 in presenting bound substrates in a specific geometric orientation.

[0465] It is peculiar that such a spindly structure is sufficient to maintain rigidity. Perhaps in the context of the dimer, additional contacts help to stabilize position of the WD repeats with respect to the other part of the protein Indeed, the N terminal dimerization domain is required for function. Or perhaps a modicum of flexibility is important for the catalytic mechanism.

[0466] Probing Substrate Selectivity Against Positively Charged Residues

[0467] Cdc4 bind Sic1 in a multi site dependent manner. Each of the phosphorylation sites in Sic1 are sub-optimal in isolation but series of 5 to 7, they work coopertively to bind to Cdc4 through an avidity effect. Part of the subs optimal character of the sites is due to the presence of Lysine in the +2 to +5 positions. From the crystal structure, the selectivity against positive residues appear to arise from electrostatic replusion from highly conserved residues on the CPD binding surface of Cdc4. To test this hypothesis, two residues not directly involved in phosphopeptide binding were mutated and then the multi site requirement for phosphoSic1 binding was evaluated (FIG. 5c).

[0468] Using an IEF pull down assay, wild type Cdc4 is shown to selectively binds to the 5,6 and 7 site phosphorylated phosphoSic1 from a pool of single to 9 site phosphorylated forms. In contrast, the double mutant binds to 3,4,5,6,7 site phosphorylated forms of Sic1 (FIG. 5a). This supports the notion of selectivity and the basis for avidity that may be important for setting sensitive threshold for cell cycle progression (FIG. 5b). The same effect was observed for a double mutant.

[0469] Cancer Causing Mutations in Drosophila and Human Cdc4

[0470] Mutations in human and fly orthologues of yCdc4 give rise to cancers (see Table below). All mis-sense mutations map to the WD40 CPD binding domain and either have been demonstrated or are predicted to perturb CPD binding function. In previous studies, two cancer cell lines tested positive for mutations at Arginine 534 and Arg 467 (Arg 534 and Arg 467 in yCdc4). In the crystal structure, these residues make a direct binding interaction with the P0 phospho group and our mutational analysis demonstrates an absolute requirement of these residues for CPD binding. In another study, two entrometrial cancerous tissue samples tested positive for mutations equivalent to Arg467 and Arg 485 in yCdc4. As f r the tumor cell line mutations, these mutations affect key residues required for CPD recognition.

[0471] Two mutations characterized in drosophila cancer include Ala118Val and Gly1132Glu, corresponding to yCdc4 positions Ser532 and Gly546 respectively. The first of these mutations, involve the substitution of a small Ala/Ser residue with a bulkier b-branched Valine residue. This may compromise CPD binding function through steric effects on the position of Arg434, Arg467, Arg534 triad. In the crystal structure, Ala/Ser is positioned centrally amongst the triad. The second drosophila mutation, Gly1132Glu, maps to β-strand 15 of propeller blade 4 in yCdc4. This position is within the core of the protein and mutation here likely acts by disrupting the overall WD40 domain fold or through local perturbations of structure that indirectly affect the phosphate binding pocket. Glycine in this position of the WD40 repeat motif is highly conserved. The temperature sensitive alleles previously characterized including Gly398Glu in propeller blade 1 and Ser438Asn in propeller blade 2 likely act by disrupting the fold in a similar manner to disrupt the overall WD fold. These are more distantly located from the CPD binding pocket.

[0472] Cancer Mutations H-cell lines Drosophila Entrometrial Orlicky Rosamond Arg534(425)Leu Ser/Ala532(1118)Val Arg467(465)His Arg534Ala Gly398Gln Arg 467(385)Cys Gly546(1132)Glu Arg485(479)Gln Arg467Ala Ser438Asn Arg485Ala Trp426Ala

[0473] Discussion

[0474] Recognition of Phosphorylated Substrates by the Ubiquitin System

[0475] Substrate selection by Cdc4. The structure of the Skp1-Cdc4-CPD complex reveals the basis for phosphorylation-dependent recognition, the specificity of which is governed by three primary determinants. The substrate phospho-threonine is locked in place by direct contacts with three conserved and essential Arg residues. The preference for hydrophobic residues at the P−1 position (and perhaps P−2 position) is enforced by a hydrophobic pocket that lines the center of the WD40 propeller. Finally, the bias against basic residues at P+2 to P+5 is established by two conserved Arg residues positioned on the top of the propeller directly in-line with the axis of the bound peptide. These conclusions are supported by mutagenesis of key residues in Cdc4 and by structure-based engineering of Cdc4 to accept sub-optimal CPD sequences.

[0476] The construction of the Cdc4 phospho-peptide binding module differs from that of known phospho-Ser/Thr binding modules in an important respect. Known phospho-recognition domains, such as 14-3-3, WW and FHA domains appear to be composed of a series of dedicated interaction sites, each of which contributes incrementally to the overall binding interaction (Yaffe and Elia, 2001). The Cdc4-substrate interaction is dominated by extensively coordinated phospho-Thr and Pro residues, as well as by a striking positive electrostatic potential around the binding site. The hydrophobic pocket that selects residues in the P−2 and P−1 positions also contributes to binding affinity. In contrast to other phospho-recognition modules, however, the strong binding of the phosphorylated residue is partially offset by specific selection against basic residues in the substrate peptide, through electrostatic repulsion from a basic patch downstream of the phosphate binding pocket. These features allow the binding affinity for any given peptide to be precisely tuned. Thus, all of the natural CPD motifs in Sic1 are sub-optimal in one or more respects; indeed only peptides derived from the T45 site exhibit any detectable interaction with Cdc4 (Nash et al., 2001). These features establish a requirement for substrate phosphorylation on multiple sites, which mediate a high affinity interaction in a manner that depends cooperatively on the number of phosphorylated residues.

[0477] In the case of wild type Sic1, at least six sites must be phosphorylated for high affinity binding by Cdc4. As shown here, mutation of the basic selection residues shifts the binding equilibrium to lower phosphorylated forms while in previous studies, it was demonstrated that introduction of a single optimal CPD into Sic1 causes premature Sic1 degradation and genome stability (Nash et al., 2001). An advantage of this system is that not only can the affinity of individual sites be tuned over a broad range, but the number and spacing of sites can be readily varied to establish a threshold for the targeting kinase. Thus Cdc4 is able to target numerous critical factors for phosphorylation-dependent degradation, including the Cdk inhibitor Sic1, the polarization factor Far1, the replication initiator Cdc6 and the transcription factor Gcn4, all of which may be controlled with different kinetics and different phosphorylation thresholds (Deshaies, 1999). These properties distinguish Cdc4 from other known phospho-peptide binding modules that typically interact with dedicated sites on their substrates through a single high affinity interaction (Pawson and Nash, 2000; Yaffe and Elia, 2001).

[0478] The mechanism that engenders a cooperative binding effect remains to be determined. In principle, multiple interactions sites might increase binding either by engaging more than one binding site on Cdc4, or by decreasing the probability of dissociation from Cdc4 (Deshaies and Ferrell, 2001; Harper, 2002; Nash et al., 2001). Cooperative interactions for the dual SH2 domain phosphatase SH-PTP2 and 14-3-3% rely on two substrate binding sites for high affinity recognition of bivalent ligands (Eck et al., 1996; Yaffe et al., 1997). Notably though, inspection of the WD40 surface does not reveal any other potential ligand binding pockets or grooves that might accommodate a phosphorylated peptide motif. Although secondary weak phospho-dependent interactions might occur, it is not obvious from the structure where such putative secondary sites might be located. In favor of the probabilistic cooperativity effect, mathematical modeling suggests that cooperative behaviour arises for the interaction between a single binding site and a polyvalent ligand as a function of the number of ligand sites. In effect multiple ligand sites increase the local concentration of ligand beyond a diffusion limited threshold for escape from the receptor. In the absence of candidate secondary sites, the simplest model is favored in which Cdc4 contains only a single phospho-dependent binding site.

[0479] Comparison to other phospho-peptide binding domains. The structure of the Cdc4 WD40 domain provides direct evidence that WD40-type repeats can assemble into propellers with more than seven blades (Fulop and Jones, 1999). One consequence of the additional blade is an enlarged channel through the center of the propeller, which creates a wide binding pocket that accommodates the core Leu-pThr-Pro ligand. This pocket contrasts to all other phospho-Ser/Thr binding domains, which engage their ligand through more shallow surface contacts within loops that extend from the core domain. WD40 domains are known to interact with other proteins in at least two different modes. In the Gb transducin and TUP1 WD40 domains, the protein interaction region occurs across the top of the propeller, much as in the case of Cdc4 (Sprague et al., 2000; Wall et al., 1995). In a second mode, defined for the WD40 domain of clathrin and the b-arrestin peptide, a “peptide-in-groove” interaction occurs on the bottom edge of the propeller between the b-strands of the second blade (ter Haar et al., 2000). Modeling of b-TrCP, which binds the consensus motif DpSGXXpS [SEQ ID NO.42] in IkBa, b-catenin, and Vpu (Yaffe and Elia, 2001), suggests that an extensive basic region on the top of the propeller will engage substrate peptides in an analogous manner to Cdc4.

[0480] Spatial orientation of SCF substrates. A conserved feature between all E3 structures solved to date is the large distance between the substrate binding site and the catalytic site (Huang et al., 1999; Zheng et al., 2002; Zheng et al., 2000). Modeling of the Skp1-Cdc4 complex onto a model of the Skp1-Cull-Rbx1-E2 complex suggests that the substrate is positioned for direct frontal attack by the E2 catalytic site but that a gap of some about 65 Å must be bridged between the two sites, presumably by the substrate polypeptide. Unexpectedly, superposition of the WD40 domain of Cdc4 with the LRR of Skp2 does not align the defined phosphopeptide binding pocket of Cdc4 with a potential phospho-recognition site of on the concave face of the LRR repeats (Zheng et al., 2002), at least as defined by mutational analysis of the related F-box protein Grr1 in yeast (Hsiung et al., 2001). If the relative position of substrates in the WD40 versus LRR class of F-box proteins differs, spatial plasticity in substrate presentation must be possible. This notion is consistent with the fact that the HIV protein Vpu is able to redirect the specificity of the F-box protein b-TrCP by bridging bTrCP to the host cell protein CD4, in a manner that depends on phospho-dependent recognition of Vpu by b-TrCP (Margottin et al., 1998). Similarly, it is possible to create synthetic adapters that bridge the substrate recognition site of an F-box protein to an ectopic substrate (Sakamoto et al., 2001). Finally, by definition all E3s must able to accommodate the substrate and the elongating ubiquitin chain generated by repeated catalytic cycles (Pickart, 2001). All of these points argue for considerable spatial leeway, and possibly flexibility of F-box protein orientations within the SCF catalytic cavity.

[0481] Based on the extensive Skp1-Skp2 interface, and on the inactivation of Cul1 by insertion of a flexible linker, it has been proposed that SCF complexes, and perhaps E3 enzymes in general, must present substrates to the catalytic site in a rigidly defined fashion (Zheng et al., 2002). However, the WD40 domain and the F-box of Cdc4 are linked only by a single α-helical stalk, with additional surface contact between the domains, all of which is mediated by non-conserved residues. It is thus somewhat difficult to reconcile the properties of the two F-box protein structures solved to date. Although it may be that regions truncated from Cdc4 to enable crystallization may normally help stabilize the interface, none of these regions are highly conserved between closely related Cdc4 family members. Perturbation of the rotational and translational position of the WD40 domain by introduction of additional residues into the stalk abrogates function in all cases, except for a long insertion of 12 residues. The fact that this gross structural change can be tolerated implies a degree of comformational plasticity with the catalytic cradle. This plasticity may facilitate the access of multiple ubiquitination sites within Sic1 to the catalytic center, as directed by the multiple low affinity CPD motifs in Sic1.

[0482] Insights into substrate recognition by human Cdc4. In metazoans, Cdc4 targets multiple critical regulators of cell division and development. Among these, cyclin E is a crucial substrate because its abundance must be strictly controlled in order to avoid precocious S phase entry and attendant genome instability (Spruck et al., 1999). Notably, it has been recently reported that mutational inactivation of hCDC4 occurs in several cancer cell lines that exhibit high levels of cyclin E (Moberg et al., 2001; Strohmaier et al., 2001). In addition, hCDC4 may be mutated in up to 30% of endometrial cancers (Spruck et al., 2002). Quite strikingly, known cancer associated mutations in hCDC4 alter phospho Thr-binding residues. Given the probable requirement for homodimerization in active SCF complexes (Kominami et al., 1998; Suzuki et al., 2000), such mutations might be expected to acts in a partial dominant negative manner. Other critical substrates that appear to bind Cdc4 in a phosphorylation dependent manner include SEL-10, a negative regulator of the LIN-12/Notch pathway (Hubbard et al., 1997) that targets the transcriptionally active Notch intracellular domain for degradation (Gupta-Rossi et al., 2002; Wu et al., 2001) and the presenilins, dominant mutations in which predispose to familial early onset Alzheimer's disease (Selkoe, 2001; Wu et al., 1998). Mutations that interfere with hCdc4 activity may therefore compound multiple disease phenotypes.

[0483] Yeast and human Cdc4 exhibit a high degree of structural similarity, especially in the critical substrate binding region, and moreover, Cdc4 family members are functionally conserved since the hCdc4 substrate cyclin E is efficiently degraded in yeast in a CDC4-dependent manner (Koepp et al., 2001; Nash et al., 2001; Strohmaier et al., 2001). The structure of yeast Cdc4 thus affords insights for rational drug design. Significantly, the low affinity of individual natural CDP sites that engender the requirement for multisite phosphorylation means that even compounds of moderate affinity can readily out-compete the binding of fully phosphorylated substrates (Nash et al., 2001). Naively, inhibition of hCdc4-substrate interactions would be expected to exacerbate the deregulated proliferation caused by stabilization of cyclinE, Notch-IC or presenilin. However, if Cdc4 or Cdc4-like activities limiting for growth, Cdc4 antagonists may have heightened toxicity in cells that are hypomorphic for Cdc4 function. Alternatively, disruption of hCdc4 function may cause synthetic lethal effects in combination with otherwise non-lethal mutations in functionally overlapping pathways (Tong et al., 2001).

EXAMPLE 2

[0484] The following methods were used in the investigation described in the example: Protein expression and purification. The Cdc4 fragment employed for crystallization was deleted for residues 1-262, 602-605, 609-624, and 745-779 to remove loop regions based on sequence alignments and limited proteolysis of the intact SCF^(Cdc4) complex. Skp1 was deleted for a non-conserved loop insertion spanning residues 37-64. A ^(GST)Skp1-^(His6)Cdc4 complex was co-expressed from plasmid pMT3169 in B934 (DE3) bacterial strain (Stratagene) cells grown in minimal media supplemented with a mixture of selenomethionine (40 μg/ml) and methionine (0.4 ug/ml) and purified by double affinity tag chromatography (Nash et al., 2001). All mutations were constructed by standard methods using oligonucleotides listed in Table 7 and sequence verified in their entirety. Mutants were sub-cloned into pMT3055 or pMT3217 for expression in bacteria or yeast, respectively, as listed in Table 8. The WD40 domain of the helix α6 linker mutants Ala1, Ala2, Ala12, and helix α6 breaker could not be stably expressed in bacteria; the Ala12 mutant also could not be expressed in yeast.

[0485] Crystallization, data collection, structure determination and modeling. Hanging drops containing 1 μl of 20 mg/ml protein and 1.2 molar equivalents of the cyclin E derived CPD peptide (acetyl-Gly-Leu-Leu-pThr-Pro-Pro-Gln-Ser-Gly-amide) [SEQ ID NO 40]in buffer (10 mM HEPES pH 7.5, 250 mM NaCl, 1 mM DTT) were mixed with equal volume of reservoir buffer (0.1 M Tris pH 8.5, 1.5 M ammonium sulphate). Crystals of the space group P3₂, (α=107.7 Å, b=107.7 Å, c=168.3 Å, α=γ=90°, β=120°), with two Cdc4-Skp1-CPD complexes in the asymmetric unit were obtained at 20° C. A Multiple Anomalous Dispersion (MAD) experiment was performed on a frozen crystal at the Advanced Photon Source (Argonne, Ill.) beamline BM 14-C and BM 14-D (λ1=0.9798 Å, λ2=0.9800 Å, λ3=0.9000 Å) using a Quantum 4 ADSC CCD detector. Data processing and reduction were carried out with the HKL program suite (Otwinowski and Minor, 1997). The programs SHARP (de La Fortelle and Bricogne, 1997) and SnB (Miller et al., 1994) were used in combination to locate and refine 19 of the total 22 selenium sites. Following phasing and density modification, a model was built using O (Jones et al., 1991) and refined to 2.7 Å resolution with NCS restraints using CNS (Brunger et al., 1998) to a working R_(value) of 23.8% and R_(free) of 27.3%. Pertinent statistics for data collection and refinement are shown in Table 2. Amino acids 37-74, and 104-115 of Skp1 and amino acids 497-507 of Cdc4 were disordered and could not be modeled. 89.1% of the residues occupy the most favored regions of the Ramachandran plot, 10.8% the additional allowed region and 0.2% the generously allowed region.

[0486] Ribbons representations were generated using Ribbons (Carson, 1991), surface representations were generated using Grasp (Nicholls et al., 1991) and electron density maps were generated using O (Jones et al., 1991). A model of the ubiquitin-E2-SCF^(Cdc4)-CPD complex was generated by superposition of the Skp1 subunits of the Skp1-Cdc4-CPD structure and the Skp1-Cul1-Rbx1 structure (PDB ID 1LDK) (Zheng et al., 2002), the RING finger domains from Rbx1 in the same Skp1-Cul1-Rbx1 complex and from the Cb1 subunit of the Cb1-UbCH7 structure (PDB ID 1FBV) (Zheng et al., 2000), and the E2 subunits of the Cb1-UbCH7 structure and an NMR-based Ubc1-ubiquitin model (PDB ID 1FXT) (Hamilton et al., 2001). The Skp1, RING domain and E2 subunits overlapped with RMSD values of 1.01 Å, 2.09 Å, and 2.04 Å respectively.

[0487] Cdc4 functional assays. CDC4 mutant alleles were assessed for complementation of a cdc4A strain in a plasmid shuffle assay (Nash et al., 2001). Sensitivity to SIC1 dosage was determined by transformation with pMT837 (GAL1-SIC1) or pMT767 (GAL1-SIC1^(T33V)) and plating on glucose medium or galactose medium. For in vitro capture of phospho-Sic1 by Cdc4, 0.5 μg of bacterially-expressed ^(HIS6)Sic1 was phosphorylated with immobilized Cln2-Cdc28 kinase from baculovirus-infected Sf9 cells and then incubated with 1 μg of immobilized wild type or mutant Cdc4²⁶³⁻⁷⁴⁴-GST-Skp1, at 4° C. for 1 hr, washed 4 times and visualized by anti-Sic1 immunoblot. For isoelectric focusing (IEF)-2D gel analyses, an evenly distributed pool of phospho-Sic1 isoforms was generated by combining different time points in a Sic1 phosphorylation reaction. 2.5 μg of the phospho-Sic1 pool was bound to 5 μg of immobilized wild type or mutant Cdc4¹⁻⁷⁴⁴-GST-Skp1. Captured isoforms were separated by denaturing IEF-2D gel electrophoresis using pH3-10NL Immobiline gel strips (Amersham) and visualized by anti-Sic1 immunoblot. Alternatively, the pool of phospho-Sic1 isoforms was incubated in solution with a ubiquitination reaction mix containing ATP, ubiquitin, yeast E1, Cdc34 and either wild type or mutant SCF^(Cdc4) complex, composed of a 1:1 ratio of bacterial Cdc4-GST-Skp1 and insect cell-produced Cdc53-Rbx1, at 30° C. for 1 h as previously described (Nash et al., 2001).

[0488] Results

[0489] Alignment of Skp1 and Cdc4 homologs from various species and limited proteolysis of full length recombinant proteins were used to deduce loop regions in Saccharomyces cerevisiae Skp1 and Cdc4 that might interfere with protein crystallization (FIG. 1). Crystals of a ternary complex of ScSkp1 bound to ScCdc4 and a CPD phosphopeptide were obtained that diffracted to a resolution of 2.7 Å (Table 2). For Skp1, a non-essential loop spanning residues 37-64 was removed. The Cdc4 fragment used extends from residues 263 to 744, which encompasses the F-box motif to the end of the WD40 domain, and was engineered to remove two predicted loop regions (FIG. 1B). This Cdc4 construct lacks an essential ˜40 reside domain that precedes the F-box in different WD40 domain containing F-box protein family embers (Wolf et al, 1999). The high affinity CPD phosphopeptide corresponds to nine residues of human cyclin E, Gly-Leu-Leu-pThr-Pro-Pro-Gln-Ser-Gly, [SEQ ID NO. 40] which binds Cdc4 with a K_(d) of 1 μM (Nash et al., 2001).

[0490] The F-box interface. Yeast Skp1 forms an elongated structure with a mixed α/β topology identical to that reported for human Skp1 (Schulman et al., 2000) and consists of a three-strand β sheet, denoted β1 to β3, and eight α-helices, denoted α1 to α8 (FIG. 2A). The structure of Cdc4 consists of an F-box domain, an α-helical linker, and a WD40 domain (FIG. 2A,B,C). The F-box domain is comprised of five α helices, denoted α0 to α4. This topology differs slightly from that reported for the F-box domain of hSkp2, which consists of a loop region L1 and three helices denoted 1 to α3 (Schulman et al., 2000) Helix α0 in Cdc4 corresponds most closely in sequence and position to the loop region L1 of hSkp2 while a half turn ant of Cdc4 helix α4 is discernable in the transition sequence between the hSkp2 F-box and the LRR domain. As observed in the hSkp1-hSkp2 complex, ScSkp1 and the F-box domain of Cdc4 associate by interdigitation of helixes α0 to α3 Cdc4 with helices α5 to α8 of Skp1, with the interface itself comprised of an inter-protein 4-helix bundle. This mode of association gives rise to a contiguous hydrophobic core that spans Skp1 and the F-box domain of Cdc4. Superposition of the yeast and human structures reveals that Skp1 helix α8 and F-box helix α4 deviate significantly in that only the first half of helix α8 is ordered in ScSkp1 and only a half turn fragment of the F-box helix α4 is apparent in hSkp2 (FIG. 6A). The difference in position and length of F-box helix α4 and Skp1 helix α8 reflects the different roles these secondary structure elements play in the linkage between their respective F-box and ligand binding domains, as described below.

[0491] The WD40 domain. Eight copies of the WD40 repeat motif in Cdc4 form an 8 blade β-propeller structure (FIG. 6B). The WD40 repeat motif of approximately 40 residues composes the outer β-strand of one propeller blade and the inner three stands of the adjacent blade in a continuous circular arrangement (Fulop and Jones, 1999). The actual Cdc4 structure contrasts to the 7 blade β-propeller predicted for Cdc4 and its orthologs based on previously solved WD40 domain structures, all of which contain only 7 blades (Koepp et al., 2001; Nash et al., 2001). This discrepancy is attributable to the cryptic nature of the 8th WD40 repeat motif. Structure based sequence alignment suggests that the WD40 domains of the F-box proteins Met30 and β-TRCP will form canonical 7-blade β-propeller structures (FIG. 1B). A variant five β-strand structure occurs in blade 2, in which a large insert in tie β12-β13 linker allows the outermost β9¹ strand to run parallel to the β9 strand. This five strand composition is unique to the fungal Cdc4 orthologs. In terms of overall structural dimensions, the WD40 domain resembles a conical frustum of 40 Å diameter top surface and 50 Å bottom surface, an overall thickness of 30 Å and a central pore of 6 Å diameter. The CPD binding site resides on the top surface of the frustum and runs across the edge of the pore, while the bottom surface of the frustum links to the F-box domain.

[0492] The F-box to WD40 domain linker. The F-box domain of Cdc4 is followed by a helical extension that forms a structured bridge to the WD40 domain. The bridge consists of two α-helices, α5 and α6, that together with helices α3 and α4 of the F-box domain form a platform and stalk-like structure that positions the WD40 domain well away from the F-box domain (FIG. 2A,C). The relative orientation of the F-box domain and WD40 domain is imposed almost entirely through the integrity of the stalk-like helix α6, which is 30 Å in length. The N-terminal end of helix α6 is anchored into the hydrophobic core of the F-box domain through interactions involving α6 residues Phe 355 and Leu 356 and F-box residues Ile 295, and Ile 296, Leu 315, Trp 316, and Leu 319 (FIG. 2C). Helix α5 packs along side the base of helix α6 opposite to the F-box domain through hydrophobic interactions involving Tyr342, Leu 338 and Leu 334. The C-terminal end of helix α6 inserts obliquely between propeller blades α7 and α8 of the WD40 domain through van der Wals and hydrophobic interactions involving residues Trp 365 and Ile 361 with WD40 domain residues Val 687, Ile 696, Leu 726 and Phe 743 in propeller blades 7 and 8. Asn 364 of helix α6 also forms a tight hydrogen bond with the backbone carbonyl group of Phe 743 in propeller blade 8. The conservation of many of these residues, with the possible exception of those within helix α5, suggests that a structured linkage between the WD40 and F-box domains may be a common feature of the WD40 family F-box proteins.

[0493] The interdomain connection between the F-box and the WD40 domains of Cdc4 appears less rigidly structured than the corresponding region in hSkp2 (FIG. 6A). Outside of the stalk helix α6, only two close contacts (<3.5 Å) are observed between the WD40 domain and other regions of Cdc4 (FIG. 2C). These contacts consist of hydrogen bonds between Asn684 and Arg700 in two loop regions of propeller blade 7 with Glu 323 in the α4-α5 linker of the helical extension. Both hydrogen bonds are maintained in the two Cdc4 molecules of the crystal asymmetric unit but all three residues are poorly conserved amongst Cdc4 orthologues (FIG. 1B). The lack of additional stabilizing interactions suggests that the F-box to WD40 domain linker is not exceedingly rigid, and indeed, the WD40 domain in the two Cdc4 molecules of the crystal asymmetric unit differ relative to their F-box domains by a 5° rotation about the long axis of helix α6. In contrast, in hSkp2 the F-box domain helix α4 terminates abruptly in an immediate transition to the LRR domain fold such that the adjoined domains form a rigid hydrophobic core (Schulman et al., 2000). Although the Skp2 and Cdc4 families of F-box proteins employ structurally divergent F-box interfaces, the general position of the WD40 and LLR domains are nonetheless similar (FIG. 6A).

[0494] Model of the SCFCd^(Cdc4)E2 complex. The structure of the Skp1-Cdc4-CPD complex sheds light on how substrates are presented by the F-box protein to the E2 for ubiquitin transfer. A complete model of the E2-SCF^(Cdc4)-substrate complex consisting of ubiquitin, hUbc7, hCul1, hRbx1, ScCdc4, ScSkp1, and the CPD peptide is shown in FIG. 6B. This model is based on the reconstructed E2-SCF^(Skp2) complex derived by Pavletich and colleagues (Zheng et al., 2002), in conjunction with an NMR-based ubiquitin-E2 thioester model (Hamilton et al., 2001). Two interesting features are apparent. First, the distance between the E2 active site cysteine and the phosphate group of the bound CPD peptide is approximately 59 Å, which is similar to the spacing reported between the substrate interaction site and the E3 catalytic site in the hUbc7-Cb1 structure (Zheng et al., 2000). Secondly, the WD40 domain presents the CPD peptide in a direct line-of-sight to the E2. Although the ligand-binding site on hSkp2 has not been determined, mutagenesis studies on the LRR-containing F-box protein Grr1 in yeast suggest that substrates bind to the inner side of the curved repeat surface (Hsiung et al., 2001). If the position of this site is maintained in hSkp2, then the LRR domain of Skp2 is predicted to project substrates in an orthogonal direction to that of the Cdc4 WD40 domain (FIG. 6A).

[0495] Phosphopeptide recognition. The CPD binding surface represents the most conserved part of the WD40 repeat domain structure (FIG. 7A-D). The central CPD sequence Leu-pThr-Pro-Pro [SEQ ID NO. 41] was modeled unambiguously in unbiased experimental electron density maps in both Skp1-Cdc4-CPD complexes of the crystal asymmetric unit (FIG. 3). Interpretable electron density is also apparent for the P−2 Leu, P+3 Gln, P+4 Ser, and P+5 Gly positions, but only in one complex of the crystal asymmetric unit. The CPD peptide binds in an extended manner across β-propeller blade 2 with the N-terminus oriented towards the central pore of the WD40 domain and the C-terminus oriented towards the outer rim. Identical substrate peptide orientations and contacts were observed for an independent Skp1-Cdc4-CPD structure with a phosphopeptide derived from the transcription factor Gcn4, which is a physiological substrate of Cdc4 in yeast (Meimoun et al., 2000; Chi et al., 2001). However, of the Gcn4 peptide sequence, Phe-Leu-Pro-pThr-Pro-Val-Leu-Glu-Asp [SEQ ID NO. 43], only the core residues Pro-pThr-Pro had discernable electron density.

[0496] The CPD sequence requirements for the CPD-Cdc4 interaction are fully accounted for by structural elements in the WD40 domain. An absolute requirement for phosphorylation at Ser or Thr at the P−0 position of the CPD derives from a network of electrostatic interactions and hydrogen bonds that coordinate the P0 pThr phosphate group (FIG. 7C, D). This interaction is mediated by residues that are conserved across all Cdc4 orthologs (FIG. 1B). The P0 phosphate group forms direct electrostatic interactions with the guanidinium groups of Arg485, Arg467, and Arg534 and a direct hydrogen bond with the side chain of Tyr548. The side chain of Tyr548 is coordinated by stacking interactions with the guanidinium group of Arg572, which in turn is coordinated by a hydrogen bond to the side chain of Tyr574. Although Cdc4 shows a 6-fold preference for pThr over pSer (Nash et al., 2001), the structural basis for this selectivity is not obvious since the Cy methyl group of Thr is directed towards solvent and does not make contact with the WD40 domain surface.

[0497] A second absolute requirement for CPD-Cdc4 interaction rests on the P+1 proline, the side chain of which projects into a three-sided pocket on the WD40 surface. One side of this pocket is formed by the side chain of Trp 426, which packs in a coplanar manner with the P+1 proline side chain. The opposite side of this binding pocket is formed by the side chain of Arg 485 via coordination of the proline side chain and backbone carbonyl group through van der Waals and hydrogen bonding interactions, respectively. The side chains of Thr 441 and Thr 465 define the remaining side of the P+1 proline binding pocket, with Cy side chain groups composing a hydrophobic surface. The hydroxyl groups of Thr 441 and 465 orient away from the P+1 binding pocket, where they are well placed to influence binding specificity for CPD residues C-terminal to the P+1 position. Unlike Trp 426 and Arg 485, which are invariant amongst the Cdc4 orthologs, Thr 441 and Thr 465 are both substituted with lie in the S. pombe Cdc4 ortholog Pop1 (FIG. 1B). This substitution might restrict CPD sequences able to bind Pop1 through steric or hydrophobic constraints on residues C-terminal to the P+1 proline position.

[0498] Cdc4 displays a strong preference for the hydrophobic residues Leu/Ile/Pro at the P−1 and Leu/Ile at the P−2 CPD positions. In the crystal structure, the P−1 Leucine side-chain fits into a hydrophobic pocket composed of invariant residues Trp 426, Trp 717, and Thr 386, and the conserved hydrophobic residue Val 384. While less precisely modeled, the main chain position of Leu−2 lies in close proximity to a third hydrophobic pocket composed of the invariant residue Tyr574, and the conserved hydrophobic residues Met 590 and Leu634. The hydrophobic character of the P−1 and P−2 pockets is manifest as selection against both charged and small polar residues at these positions in the CPD consensus (Nash et al., 2001).

[0499] The WD40 phospho-recognition domain of Cdc4 is unusual in that it exhibits strong selectivity against either Arg or Lys residues in the P+2 to P+5 CPD positions, but otherwise shows no sequence preference at these positions (Nash et al., 2001). In the crystal structure, the side chain of P+2 Pro is directed towards solvent, while the main chain conformation of Pro+1 and Pro+2 causes the CPD to kink away from the peptide-binding surface from the Pro+2 position onward. As a result, only one additional contact with Cdc4 is made by the CPD following the Pro+1 position, namely a weak hydrogen bond with sub-optimal geometry between the P+4 Gin side chain and the side chain of Arg 485. Because the P+1 Pro main chain is forced away from the WD40 domain surface, the selection against basic residues in the P+2, +3, +4 and +5 positions in the CPD consensus is almost certainly due to through-space electrostatic repulsion. This effect arises from a dominant positive electrostatic potential generated by both the invariant triad of Arg residues that comprise the core pThr-Pro binding pocket, and by a radial extension of the surface due to Arg 572, Arg 443 and Lys 402, the former two of which are conserved amongst Cdc4 orthologs (FIG. 7B).

[0500] A number of natural mutations detected in metazoan orthologs of Cdc4 corroborate the structure-based analysis. Two ovarian cancer cell lines bear missense mutations at conserved Arg residues that correspond to Arg 467 and Arg 534 in yeast Cdc4 (Moberg et al., 2001). In the crystal structure, these residues make direct contact with the P0 phosphate group and are essential for function (FIG. 7C, D). In a recent study of human primary endometrial tumors, mutations in phosphate-binding Arg residues equivalent to Arg 467 and Arg 485 were detected in 2 of 13 tumor samples (Spruck et al., 2002). Other cancer-associated nonsense and frameshift mutations truncate hCdc4 within the WD40 domain (Moberg et al., 2001; Strohmaier et al., 2001; Spruck et al., 2002). Similarly, all three characterized mutations in the Drosophila ago gene that lead to excess cell proliferation affect the WD40 domain (Moberg et al., 2001). One of these mutations, Ala1118Val, corresponding to position SerS32 in ScCdc4 substitutes a conserved small residue with a bulkier residue at the center of the critical Arg 434-Arg467-Arg534 triad (FIG. 7C).

[0501] Mutational analysis of the F-box to WD40 domain linker. To probe the importance of orientation and rigidity in the F-box WD40 inter-domain linker, point mutations, insertions or deletions were introduced into the platform and stalk structure of Cdc4. None of these deletions affected the ability of the recombinant proteins to bind phospho-Sic1 in vitro or protein abundance in vivo (FIG. 8A and data not shown). Introduction of the helix destabilizing residues glycine and proline into helix α5 did not compromise Cdc4 function in vivo (FIG. 8B), consistent with the poorly conserved nature of this region (FIG. 1B). However, two different deletions of helix α5 eliminated Cdc4 function in vivo, indicating that the F-box-WD40 domain interface is an essential structural component. Similarly, placement of helix destabilizing residues at the center of helix α6 or the lengthening of this helix by the insertion of one, two, three, four, 8 or 12 amino acid residues disrupted Cdc4 function in vivo. Helix α6 is thus critical for productive orientation of the WD40 domain.

[0502] Mutational analysis of the CPD binding surface. Previous mutational analysis based on sequence conservation in the Cdc4 family identified Arg467, Arg485 and Arg534 as essential for substrate binding and function in yeast (Nash et al., 2001). Two of the three corresponding residues in hCdc4, Arg 417 and Arg 457, are essential for the binding of phospho-cyclin E, while the third corresponding to Arg485 was not tested (Koepp et al., 2001). To systematically probe the role of residues that form the highly conserved peptide binding surface, a panel of Cdc4 mutants was generated and each were tested for pSic1 binding in vitro, complementation of a cdc4A strain and sensitivity to increased SIC1 dosage. Four mutants, Arg467Ala, Arg485Ala, Arg534Ala, and Trp426Ala were unable to bind phospho-Sic1 in vitro or complement a cdc4A strain, but were fully competent for Skp1 binding (FIG. 8A, B). The essential function of these residues is not confined to elimination of Sic1 because none of the corresponding mutant alleles were able to rescue a cdc4Δ sic1Δ strain. These results reflect the critical structural role played by these residues in coordination of the P0 phosphate and the P+1 proline of the CPD. Mutation of the remaining phosphate-coordinating residue, Tyr548, did not cause loss of viability but did result in dosage sensitivity to SIC^(Thr)33Val, which encodes a partially stabilized version of Sic1 (FIG. 8C). Mutation of Arg 572 had the same effect, as befits the observed stacking interaction between this residue and Tyr 548. Although both mutants were severely impaired for binding to phospho-Sic1 in vitro, this effect may be exacerbated by the tendency of these recombinant proteins to aggregate. In summary, the six residues that directly or indirectly coordinate the primary pThr-Pro core motif are critical for CPD recognition in vitro and Cdc4 function in vivo.

[0503] Disruption of residues that confer selection at the P−2, P−1 and P+2 to P+5 positions had only modest effects on the ability of Cdc4 to target pSic1. A Trp717Asn mutation predicted to disrupt the P−1 pocket conferred sensitivity to dosage of SIC1^(Thr33Val), but did not overtly affect the pSic1-Cdc4 interaction in vitro. Individual mutations in all other residues that are well positioned to affect substrate selection, namely Arg443Ala, Arg443Asp, Lys402Ala, Tyr574Phe and Val384Asn were indistinguishable from wild type in each of the assays used. Substrate selection residues on the WD40 surface thus contribute only modestly if at all to the essential function of Cdc4. As described below, however, these residues play a subtle but critical role in setting the phosphorylation threshold for the CPD-Cdc4 interaction.

[0504] Modulation of CPD substrate selectivity. A critical feature of the Sic1-Cdc4 interaction is the requirement for phosphorylation of Sic1 on multiple sites. To enforce this requirement, each of the phosphorylation sites in the native Sic1 sequence are sub-optimal in one or more respects (FIG. 9A). The Cdc4-CPD structure suggests that selectivity against basic residues may be due to electrostatic repulsion generated from the conserved patch of basic residues in and around the CPD binding pocket, while selection for hydrophobic residues arises from the P−1 pocket that is composed in part by Val 384 and Trp717. To examine the basis for selection against sub-optimal CPD motifs, the effects of mutations in non-essential residues in these two regions on the multisite phosphorylation requirement for Sic1 recognition were assessed.

[0505] The ability of Cdc4 to capture various phosphoisoforms of wild type Sic1 from a pool of recombinant Sic1 that had been phosphorylated to various extents by Cln2-Cdc28 was monitored. As resolved by isoelectric focusing, this pool contained roughly equal amounts of Sic1 phosphorylated on 1, 2, 3, 4, 5, 6, 7, 8 and 9 sites. Wild type Cdc4 was only able to capture Sic1 phosphorylated on six or more sites (FIG. 9B). This result formally demonstrates the transition in binding affinity between 5 and 6 phosphorylation sites, as initially inferred from capture of a series of Sic1 phosphorylation site mutants by Cdc4 (Nash et al., 2001). The role of positive electrostatic potential in selecting against sub-optimal CPD sequences with basic residues at C-terminal positions was tested with the Lys402Ala Arg443Asp double mutant. This mutant was able to select Sic1 phosphoisoforms that contained as few as three phosphorylation sites (FIG. 9B). The ability of the Lys402Ala Arg443Asp double mutant to capture lower phosphorylated forms of Sic1 is also evident in one-dimensional SDS-PAGE (FIG. 8A). Similarly, perturbation of the P−1 hydrophobic pocket with a Val384Asn Trp717Asn double mutation allowed capture of Sic1 phosphorylated on as few as four sites. These in vitro binding results were recapitulated in solution-based in vitro ubiquitination assays with wild type and mutant forms of Cdc4. Both double mutant forms of Cdc4 were able to convert Sic1 phosphoryated on four or five sites to oligo-ubiquitinated species, whereas wild type Cdc4 was unable to do so (FIG. 9C). The double mutants were, however, less efficient than wild type at elaborating fully ubiquitinated species of phospho-Sic1, perhaps because of protein stability effects or interference with catalytic steps after substrate binding. This interpretation is consistent with the sensitivity of strains bearing the double mutant alleles to SIC1^(Thr33Val) dosage (FIG. 8B). Overall, re-engineering of negative selection residues in the Cdc4 WD40 domain supports the notion that the series of sub-optimal CPD motifs in Sic1 sets a high phosphorylation threshold for its recognition by Cdc4.

[0506] Discussion

[0507] The structure of the Skp1-Cdc4-CPD complex provides direct visualization of substrate orientation within an SCF complex. Insights gained from the structure include the unexpectedly frail interface between the F-box and the WD40 repeat domain, the basis for dedicated pThr-Pro dipeptide recognition by a novel eight-blade WD40 propeller, and a detailed understanding of the basis for selection against natural CPD sequences. The latter feature appears to be tailored to enforce multisite phosphorylation dependent degradation of Sic1, which in turn would help engender a highly cooperative onset of DNA replication (Nash et al., 2001). Similar principles may well operate for other Cdc4 substrates, including cyclin E, Notch^(IC) and presenilin in mammalian cells (Strohmaier et al., 2001; Lai, 2002; Selkoe, 2001). Because yeast and human Cdc4 are structurally and functionally analogous (Nash et al., 2001; Strohmaier et al., 2001; Koepp et al., 2001), the structure of yeast Cdc4 affords obvious insights for pharmacological modulation of hCdc4 function in these pathways. Interestingly, a significant proportion of characterized human and fly CDC4 mutations alter residues in the CPD binding pocket. Given the probable requirement for homodimerization in active SCF complexes (Wolf et al., 1999), such mutations might act in a partial dominant negative manner to confer a growth advantage in the heterozygous state.

[0508] Phospho-recognition by Cdc4. The specificity of phosphorylation-dependent recognition by the WD40 domain of Cdc4 is governed by three main determinants: (i) a dedicated pThr-Pro binding pocket; (ii) a deep hydrophobic pocket that selects hydrophobic residues N-terminal to the phosphorylation site, and (iii) a through space electrostatic selection against basic residues C-terminal to the phosphorylation site. As for all documented phospho-dependent lipid/protein recognition modules, the Cdc4 WD40 domain employs arginine residues to directly contact the phosphate group of the ligand. However, unlike most domains in which adjacent residues impose subtle effects on specificity (Yaffe and Elia, 2001), the P+1 proline is an integral component of the core binding determinant (Nash et al., 2001). In the Cdc4-CPD co-crystal, ligand residues are locked in place by direct contact of the phosphate and proline carbonyl groups with three conserved and essential Arg residues, while the proline side chain inserts into a tight hydrophobic pocket formed by Trp426, Thr441, and Thr465. Because the phospho-binding pocket infrastructure has no obvious demarcation between the pThr and Pro binding sites, the Cdc4 WD40 domain is in effect a dedicated pThr-Pro binding module.

[0509] Comparison to other peptide recognition modules. Interesting parallels can be drawn between the Cdc4 WD40 domain, 14-3-3 domains and the class IV WW domains, which all have the ability to recognize phospho-Ser/Thr epitopes in the context of adjacent proline residues (Yaffe and Elia, 2001). The interaction of the Pin1 class IV WW domain with a pSer-Pro peptide differs from Cdc4 in that it does not rely on an extensive network of Arg residues for phosphate coordination (Verdecia et al., 2000). However, a striking similarity between Pin1 and Cdc4 lies in the P+1 proline binding pocket, which in both cases depend on a highly conserved tryptophan side chain to engage the P+1 proline pyrrolidine ring through a coplanar interaction. In contrast to Cdc4, Pin1 actually displays a preference for Arg in the P+2 position, such that the binding specificity of the pSer-Pro recognition domain closely matches that of the targeting CDK enzymes.

[0510] 14-3-3 domains bind pSer epitopes with a preference, but not an absolute requirement, for proline residues at the P+2 position (Yaffe et al., 1997). This less stringent selection arises because the 14-3-3 proline binding pocket is able to accommodate other residues with propensity to form β-turns. Interestingly, the proline preferences in both the 14-3-3 and Cdc4 WD40 domains give rise to the same qualitative effect: in each case the prolines terminate direct interactions between the peptide and the ligand binding domain by orienting the peptide away from the domain surface. In the case of Cdc4, biologically significant electrostatic effects operate in spite of the loss of direct peptide contact. Physiologically relevant substrate anti-selection mediated by charge repulsion is unique amongst known protein interaction modules.

[0511] The structure of the Cdc4 WD40 domain provides direct evidence that WD40-type repeats can assemble into propellers with more than seven blades (Fulop and Jones, 1999). WD40 domains are known to interact with other proteins in at least two different modes, either across the front face of the propeller, as in the case of Cdc4, or on the outer edge of the propeller as in the case of clathrin (ter Haar et al., 2000). Modeling of the F-box protein P-TrCP, which binds the doubly phosphorylated consensus motif DpSGXXpS [SEQ ID NO. 42] in IκβBβ-catenin, and Vpu (Yaffe and Elia, 2001), reveals an extensive conserved basic region on the front face of the propeller, which may engage substrate phosphoepitopes in an analogous manner to Cdc4.

[0512] Spatial orientation of SCF substrates. A conserved feature between all E3 structures solved to date is the substantial distance between the substrate binding site and the catalytic site (Huang et al., 1999; Zheng et al., 2000; Zheng et al., 2002). Superposition of the Skp1-Cdc4 complex onto a model of the Skp1-Cull-Rbx1-E2-ubiquitin complex suggests that the substrate is positioned for direct frontal attack by the E2 catalytic site, but that a gap of some 59 Å between the two sites must be bridged, presumably by the substrate polypeptide. The disordered structure of Sic1 lends itself to this possibility (Nash et al., 2001). Intriguingly, overlay of the WD40 domain of Cdc4 with the LRR of Skp2 does not align the defined phosphopeptide binding pocket of Cdc4 with a potential phospho-recognition site on the concave face of the LRR repeats (Zheng et al., 2002), at least as defined by mutational analysis of the related F-box protein Grr1 in yeast (Hsiung et al., 2001). If the relative position of substrates in the WD40 versus LRR class of F-box proteins do in fact differ, spatial leeway in substrate presentation must be possible.

[0513] Based on the extensive Skp1-Skp2 interface, and on the inactivation of Cull by insertion of a flexible linker, it has been proposed that SCF complexes, and perhaps E3 enzymes in general, must present substrates to the catalytic site in a rigidly defined fashion (Zheng et al., 2002). Unexpectedly, the WD40 domain and the F-box of Cdc4 are linked only by a single α-helical stalk, with very limited additional contacts. Despite the lack of sequence conservation in the a helix 6 structure that supports the WD40 domain, spatial constraints are nevertheless evident, as shown by the sensitivity of the structure to rotational and translational shifts caused by insertion of additional residues into the stalk. It is also possible that regions truncated from Cdc4 to enable crystallization may normally help stabilize the inter-domain interface.

[0514] Cooperativity in substrate selection by Cdc4. The properties of the Cdc4 phosphopeptide binding module differ from those of other known modules in the important respect that the interaction with core recognition elements is partially offset by specific selection against basic residues in the substrate peptide. This feature establishes an intrinsic antagonism between the recognition mechanism and the targeting CDK kinases, which prefer Ser/Thr-Pro sites with C-terminal basic residues (Endicott et al., 1999). Significantly, all of the natural CPD motifs in Sic1 contain one or more mismatches to the optimal CPD consensus. This system based on positive and negative ligand selection may not only set an elevated threshold for kinase activity, but may also allow the threshold to be precisely tuned for any given substrate by varying the number, spacing and properties of each site. Thus, Cdc4 is able to target numerous critical factors for phosphorylation-dependent degradation, including the Cdk inhibitor Sic1, the CDK inhibitor and polarization factor Far1, the replication initiator Cdc6 and the transcription factor Gcn4, all of which may be controlled with different kinetics and different phosphorylation thresholds (Patton et al., 1998). In one extreme, typified by Gcn4 and cyclin E, the substrate may contain a high affinity site that is augmented by several minor low affinity sites (Meimoun et al., 2000; Chi et al., 2001; Strohmaier et al., 2001). In the other, more akin to Sic1, a large number of weak sites may cooperate to drive high affinity binding only when a phosphorylation threshold is reached. As shown here, mutation of either the distal basic selection region or the P−1 pocket in Cdc4 shifts the binding equilibrium to lower phosphorylated forms of Sic1, which, in the absence of other structural effects that may compromise Cdc4, would be predicted to cause premature DNA replication and genome stability (Nash et al., 2001). These features distinguish Cdc4 from other known phospho-peptide binding modules characterized to date that typically interact with dedicated sites on their substrates through a single high affinity interaction.

[0515] The mechanism that underlies the cooperative binding transition of the phospho-Sic1-Cdc4 interaction between five and six phosphorylation sites remains to be determined. In principle, multiple interactions sites might increase binding by engaging more than one binding site on Cdc4 (FIG. 9D). This type of cooperative interaction is common in biological systems, as in the avidity of antibodies for polyvalent ligands and pathogen-host interactions (Mammen et al., 1998). Analogous cooperative binding interactions occur in signaling pathways. For instance, the dual SH2 domain phosphatase SH-PTP2 and the 14-3-3ζ protein both engage two substrate binding sites on their respective ligands (Eck et al., 1996; Yaffe et al., 1997). However, inspection of the Cdc4 WD40 domain surface does not reveal any obvious ligand binding sites that might accommodate a second phosphorylated peptide motif, nor is there any biochemical evidence for secondary binding sites (Nash et al., 2001). In addition, the wide range of substrates and site spacing accommodated by Cdc4, including random concatamers of synthetic CPD sites (Nash et al., 2001), is a priori difficult to explain by two or more fixed binding sites on Cdc4.

[0516] Instead, a model is favored that requires only a single phospho-dependent binding site on Cdc4 (FIG. 9D). In this scheme, phosphorylation of multiple CPD sites on Sic1 increases the local concentration of sites around Cdc4 once the first CPD site is bound, to the point where diffusion limited escape from the receptor is overwhelmed by the probability of re-binding of any one CPD site. In a sense, Sic1 becomes kinetically trapped in close proximity to Cdc4. Mathematical modeling of an idealized polyvalent ligand-monovalent receptor interaction indicates that the rate of ligand escape from the receptor exhibits a negative exponential dependence on the number of ligand sites. The term allovalent is proposed to describe the ability of multiple weak spatially separated ligand sites to cooperatively interact with a single receptor site. The prevalence of multisite phosphorylation (Cohen, 2000), and indeed of polyvalent ligands in general (Mammen et al., 1998), suggests that this type of behavior may underlie many biological processes.

[0517] The present invention is not to be limited in scope by the specific embodiments described herein, since such embodiments are intended as but single illustrations of one aspect of the invention and any functionally equivalent embodiments are within the scope of this invention. Indeed, various modifications of the invention in addition to those shown and described herein will become apparent to those skilled in the art from the foregoing description and accompanying drawings. Such modifications are intended to fall within the scope of the appended claims. In particular it will be appreciated that the references to specific amino acid residues for particular a SCF complexes, and components thereof (e.g. F-box protein) illustrated in the Tables and Figures, in no way limits the scope of the invention and it will be appreciated that a person skilled in the art could determine the specific corresponding amino acid residues for other SCF complexes and components thereof.

[0518] All publications, patents and patent applications referred to herein are incorporated by reference in their entirety to the same extent as if each individual publication, patent or patent application was specifically and individually indicated to be incorporated by reference in its entirety. All publications, patents and patent applications mentioned herein are incorporated herein by reference for the purpose of describing and disclosing the cell lines, vectors, methodologies etc. which are reported therein which might be used in connection with the invention. Nothing herein is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention.

[0519] It must be noted that as used herein and in the appended claims, the singular forms “a”, “an”, and “the” include plural reference unless the context clearly dictates otherwise. Thus, for example, reference to “a host cell” includes a plurality of such host cells, reference to the “antibody” is a reference to one or more antibodies and equivalents thereof known to those skilled in the art, and so forth. TABLE 1 Data Collection, Structure Determination, and Refinement Statistics Peak Inflection Remote Wavelength (Å) 0.9798 0.9800 0.9000 Resolution (Å) 2.8 2.9 2.7 R_(sym) (%)  5.9 (38.7)  6.1 (36.1)  5.0 (28.9) Total Reflections 311509 187010 298371 Unique Reflections 107167 96027 116218 Completeness (%) 99.8 (99.1) 99.3 (98.3) 97.7 (93.6) I/σ 9.9 (2.7) 7.4 (2.1) 10.1 (2.9)  Phasing Power Refinement statistics Resolution range (Å) 20-2.8 Reflections 103863 R_(factor)/R_(free) (%) 24.09/28.71 Rms deviations Bonds (Å) 0.0091 Angles (°) 1.3453

[0520] TABLE 2 Data Collection, Structure Determination, and Refinement Statistics Peak Inflection Remote Phasing Statistics Wavelength (Å) 0.9798 0.9800 0.9000 Resolution (Å) 2.8 (2.9-2.8) 2.9 (3.0-2.9) 2.7 (2.8-2.7) R_(sym) (%)  5.9 (37.2)  6.1 (36.1)  5.0 (28.9) Total Reflections 311509 187010 298371 Unique Reflections 107167 96027 116218 Completeness (%) 99.8 (99.1) 99.3 (98.3) 97.7 (93.6) I/σ 9.9 (2.7) 7.4 (2.1) 10.1 (2.9)  Phasing Power 5.2/1.3 4.0/0.94 0/0.91 (ISO/ANO) Refinement statistics (remote wavelength) Resolution range (Å) 20-2.7 # protein 9364 atoms Reflections 113960 # water 72 molecules R_(factor)/R_(free) (%) 23.8/27.3 Rms deviations Bonds (Å) 0.0089 Angles (°) 1.42

[0521] TABLE 3 Atomic Contacts of a Substrate Binding Pocket No. of Atomic CDC4 WD40 Motif CDC4 atomic CPD Motif Interaction Atomic Contact Contact Atomic Contact 1 Ile 295 Phe 255 Ile296 Leu356 Leu 315 Trp 316 Leu 319 2 Val 687 Trp 365 Ile 696 Ile 364 Leu 726 Phe 743 3 Phe 743 Asn 364 4 Asn 684 Glu 323 Arg 700 5 Arg 485 PO pTyr Arg 467 Phosphate Arg 534 Tyr 548 6 Trp 426 P + 1 Proline side Arg 485 chain Thr 386 Thr 441 Thr 465 7 Trp 426 P + 1 Leucine side Trp 717 chain Thr 386 Val 384 8 Tyr 574 Leucine + 2 Thr 386 Val 384

[0522] TABLE 4 Atomic Contacts of a Substrate Binding Pocket No. of CDC4 WD40 Atomic Atomic Motif/F-box Domain CDC4 atomic CPD Motif Interaction Interaction Atomic Contact Contact Atomic Contact Property 1 Ile 295 Phe 355 hydrophobic Ile296 Leu356 interactions and Leu 315 van der Wals Trp 316 interactions Leu 319 2 Val 687 Trp 365 van der Wals and Ile 696 Ile 361 hydrophobic Leu 726 interactions Phe 743 3 Phe 743 Asn 364 hydrogen bond 4 Asn 684 Glu 323 hydrogen bonds Arg 700 5 Arg 485 PO pTyr or pSer electrostatic Arg 467 Phosphate at P-O interactions Arg 534 position of CPD hydrogen bond Tyr 548 6 Trp 426 P + 1 Proline side hydrogen and van Arg 485 chain and der Wals Thr 441 backbone carbonyl hydrophobic Thr 465 of CPD interations 7 Trp 426 P − 1 Leucine (or hydrophobic Trp 717 Ile/Pro) side chain interactions Thr 386 Val 384 8 Tyr 574 Leucine − 2 hydrophobic Met 590 Leu/Ile at P − 2 interactions Leu 634 position 9. Tyr 342 hydrophobic Leu 338 interactions Leu 334

[0523] TABLE 5 Determinants of pThr-Pro binding P-Sic1 gal gal gal pull down Sic1 wt Sic1T45A Sic1T33V gal Sic1-7 gal Sic1-6 gal Sic1-5 gal Sic1-4 gal Sic1-3 shuffle WT bind alive dead alive alive

R443A bind alive dead alive alive

R467A no bind dead R485A no bind dead R534A no bind dead R572A no bind alive dead dead alive

alive W426A no bind dead V384N bind alive dead alive alive K402A bind alive dead alive alive R443D bind alive dead alive alive Y548F no bind alive dead dead alive Y574F bind alive dead alive alive W717N bind alive dead dead alive T441I/T465I (in progress) (in progress) K402A/R443D bind alive dead dead alive W717N/V384N bind alive dead dead alive quad (in progress) dead

[0524] TABLE 6 REMARK peptide link removed (applied DPEP) : from A  31  to A  45 REMARK peptide link removed (applied DPEP) : from A  73  to A  86 REMARK peptide link removed (applied DPEP) : from B  496  to B  508 REMARK peptide link removed (applied DPEP) : from C  31  to C  45 REMARK peptide link removed (applied DPEP) : from C  73  to C  86 REMARK peptide link removed (applied DPEP) : from D  496  to D  508 REMARK peptide link removed (applied DPPP) : from E  4  to E  5 REMARK coordinates from minimization and B-factor refinement REMARK refinement resolution: 20 - 2.8 A REMARK starting r= 0.2415 free_r= 0.2846 REMARK final r= 0.2409 free_r= 0.2871 REMARK rmsd bonds= 0.009114 rmsd angles= 1.34531 REMARK B rmsd for bonded mainchain atoms= 1.230 target= 1.5 REMARK B rmsd for bonded sidechain atoms= 1.778 target= 2.0 REMARK B rmsd for angle mainchain atoms= 2.103 target= 2.0 REMARK B rmsd for angle sidechain atoms= 2.675 target= 2.5 REMARK target= mlf final wa= 2.77695 REMARK final rweight= 0.1078 (with wa= 2.77695) REMARK md-method= torsion annealing schedule= constant REMARK starting temperature= 2000 total md steps= 1 * 100 REMARK cycles= 2 coordinate steps= 20 B-factor steps= 10 REMARK sg= P3(2) a= 107.669 b= 107.669 c= 168.3 alpha= 90 beta= 90 gamma= 120 REMARK topology file 1 : CNS_TOPPAR:protein.top REMARK topology file 2 : CNS_TOPPAR:dna-rna.top REMARK topology file 3 : CNS_TOPPAR:water.top REMARK topology file 4 : CNS_TOPPAR:ion.top REMARK topology file 5 : CNS_TOPPAR:tpo.top REMARK parameter file 1 : CNS_TOPPAR:protein_rep.param REMARK parameter file 2 : CNS_TOPPAR:dna-rna_rep.param REMARK parameter file 3 : CNS_TOPPAR:water_rep.param REMARK parameter file 4 : CNS_TOPPAR:ion.param REMARK parameter file 5 : CNS_TOPPAR:tpo.param REMARK molecular structure file: automatic REMARK input coordinates: 36modl.pdb REMARK reflection file= remote.cv REMARK ncs= none REMARK B-correction resolution: 6.0 - 2.8 REMARK initial B-factor correction applied to fobs : REMARK B11= 1.580 B22= 1.580 B33= −3.160 REMARK B12= −3.767 B13= 0.000 B23= 0.000 REMARK B-factor correction applied to coordinate array B: 0.915 REMARK bulk solvent: density level= 0.324998 e/A{circumflex over ( )}3, B-factor= 34.4718 A+E,+CIR  2 REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflections with |Fobs|> 10000 * rms(Fobs) rejected REMARK anomalous diffraction data was input REMARK theoretical total number of refl. in resol. range: 107240 (100.0%) REMARK number of unobserved reflections (no entry or |F|=0): 3377 (3.1%) REMARK number of reflections rejected: 0 (0.0%) REMARK total number of reflections used: 103863 (96.9%) REMARK number of reflections in working set: 93784 (87.5%) REMARK number of reflections in test set: 10079 (9.4%) CRYST1 107.669 107.669 168.300 90.00 90.00 120.00 P 32 REMARK FILENAME=“ref37.pdb” REMARK DATE:28-Jun-2002 13:23:24 created by user: orlicky REMARK VERSION:1.1 ATOM 1 CB SER A 2 72.279 75.039 74.638 1.00 40.45 A ATOM 2 OG SER A 2 72.875 75.230 73.368 1.00 36.62 A ATOM 3 C SER A 2 70.142 75.473 73.446 1.00 40.01 A ATOM 4 O SER A 2 69.547 74.397 73.338 1.00 39.92 A ATOM 5 N SER A 2 70.277 75.520 76.026 1.00 40.09 A ATOM 6 CA SER A 2 70.953 75.797 74.713 1.00 40.80 A ATOM 7 N ASN A 3 70.145 76.398 72.482 1.00 38.91 A ATOM 8 CA ASN A 3 69.428 76.196 71.221 1.00 37.67 A ATOM 9 CB ASN A 3 68.480 77.367 70.926 1.00 38.01 A ATOM 10 CG ASN A 3 67.193 77.305 71.736 1.00 38.13 A ATOM 11 OD1 ASN A 3 66.616 76.236 71.944 1.00 38.39 A ATOM 12 ND2 ASN A 3 66.733 78.458 72.184 1.00 36.20 A ATOM 13 C ASN A 3 70.310 75.996 69.990 1.00 35.89 A ATOM 14 O ASN A 3 71.503 76.275 69.995 1.00 34.48 A ATOM 15 N VAL A 4 69.685 75.500 68.928 1.00 36.46 A ATOM 16 CA VAL A 4 70.343 75.275 67.639 1.00 33.96 A ATOM 17 CB VAL A 4 70.545 73.750 67.383 1.00 33.36 A ATOM 18 CG1 VAL A 4 70.533 73.449 65.916 1.00 33.70 A ATOM 19 CG2 VAL A 4 71.855 73.295 67.985 1.00 34.50 A ATOM 20 C VAL A 4 69.415 75.889 66.584 1.00 31.88 A ATOM 21 O VAL A 4 68.209 76.036 66.818 1.00 31.04 A ATOM 22 N VAL A 5 69.972 76.282 65.443 1.00 31.25 A ATOM 23 CA VAL A 5 69.146 76.853 64.376 1.00 31.10 A ATOM 24 CB VAL A 5 69.458 78.346 64.086 1.00 31.85 A ATOM 25 CG1 VAL A 5 68.586 78.825 62.927 1.00 32.81 A ATOM 26 CG2 VAL A 5 69.188 79.192 65.314 1.00 31.47 A ATOM 27 C VAL A 5 69.339 76.075 63.089 1.00 29.35 A ATOM 28 O VAL A 5 70.448 75.952 62.588 1.00 29.57 A ATOM 29 N LEU A 6 68.232 75.561 62.574 1.00 28.63 A ATOM 30 CA LEU A 6 68.206 74.777 61.355 1.00 28.72 A ATOM 31 CB LEU A 6 67.299 73.558 61.559 1.00 27.60 A ATOM 32 CG LEU A 6 67.585 72.619 62.739 1.00 25.63 A ATOM 33 CD1 LEU A 6 66.684 71.402 62.592 1.00 24.10 A ATOM 34 CD2 LEU A 6 69.043 72.205 62.781 1.00 21.89 A ATOM 35 C LEU A 6 67.667 75.632 60.208 1.00 28.54 A ATOM 36 O LEU A 6 66.577 76.200 60.316 1.00 28.48 A ATOM 37 N VAL A 7 68.416 75.740 59.112 1.00 27.74 A ATOM 38 CA VAL A 7 67.945 76.548 57.978 1.00 25.90 A ATOM 39 CB VAL A 7 69.092 77.413 57.366 1.00 25.69 A ATOM 40 CG1 VAL A 7 68.515 78.450 56.403 1.00 25.12 A ATOM 41 CG2 VAL A 7 69.889 78.077 58.450 1.00 22.70 A ATOM 42 C VAL A 7 67.374 75.650 56.869 1.00 24.30 A ATOM 43 O VAL A 7 68.069 74.768 56.337 1.00 21.91 A ATOM 44 N SER A 8 66.111 75.881 56.522 1.00 23.21 A ATOM 45 CA SER A 8 65.453 75.091 55.486 1.00 23.15 A ATOM 46 CB SER A 8 63.966 75.433 55.375 1.00 21.22 A ATOM 47 OG SER A 8 63.794 76.735 54.826 1.00 20.44 A ATOM 48 C SER A 8 66.093 75.428 54.167 1.00 25.17 A ATOM 49 O SER A 8 66.851 76.389 54.054 1.00 27.53 A ATOM 50 N GLY A 9 65.782 74.635 53.155 1.00 26.78 A ATOM 51 CA GLY A 9 66.329 74.914 51.847 1.00 26.99 A ATOM 52 C GLY A 9 65.726 76.208 51.320 1.00 27.95 A ATOM 53 O GLY A 9 66.120 76.682 50.256 1.00 29.65 A ATOM 54 N GLU A 10 64.762 76.782 52.039 1.00 26.66 A ATOM 55 CA GLU A 10 64.160 78.025 51.582 1.00 25.22 A ATOM 56 CB GLU A 10 62.637 77.927 51.610 1.00 24.78 A ATOM 57 CG GLU A 10 62.045 76.721 50.905 1.00 24.26 A ATOM 58 CD GLU A 10 60.543 76.567 51.203 1.00 27.17 A ATOM 59 OE1 GLU A 10 59.747 77.407 50.727 1.00 27.67 A ATOM 60 OE2 GLU A 10 60.144 75.617 51.929 1.00 28.38 A ATOM 61 C GLU A 10 64.598 79.236 52.416 1.00 25.50 A ATOM 62 O GLU A 10 63.853 80.213 52.538 1.00 24.72 A ATOM 63 N GLY A 11 65.794 79.164 52.995 1.00 25.06 A ATOM 64 CA GLY A 11 66.299 80.264 53.792 1.00 25.04 A ATOM 65 C GLY A 11 65.740 80.473 55.192 1.00 25.64 A ATOM 66 O GLY A 11 66.399 81.110 56.016 1.00 25.60 A ATOM 67 N GLU A 12 64.552 79.946 55.483 1.00 26.56 A ATOM 68 CA GLU A 12 63.945 80.113 56.806 1.00 27.47 A ATOM 69 CB GLU A 12 62.510 79.614 56.782 1.00 26.92 A ATOM 70 CG GLU A 12 61.661 80.451 55.874 1.00 32.01 A ATOM 71 CD GLU A 12 60.215 80.003 55.841 1.00 35.92 A ATOM 72 OE1 GLU A 12 59.912 78.942 55.244 1.00 37.74 A ATOM 73 OE2 GLU A 12 59.367 80.716 56.419 1.00 39.01 A ATOM 74 C GLU A 12 64.705 79.459 57.951 1.00 28.74 A ATOM 75 O GLU A 12 65.222 78.345 57.826 1.00 29.61 A ATOM 76 N ARG A 13 64.804 80.170 59.069 1.00 29.55 A ATOM 77 CA ARG A 13 65.513 79.615 60.207 1.00 30.68 A ATOM 78 CB ARG A 13 66.457 80.651 60.832 1.00 32.30 A ATOM 79 CG ARG A 13 66.654 81.907 60.002 1.00 34.52 A ATOM 80 CD ARG A 13 67.459 82.959 60.756 1.00 35.08 A ATOM 81 NE ARG A 13 68.816 82.514 61.051 1.00 36.91 A ATOM 82 CZ ARG A 13 69.454 82.778 62.188 1.00 37.09 A ATOM 83 NH1 ARG A 13 68.846 83.485 63.129 1.00 35.87 A ATOM 84 NH2 ARG A 13 70.691 82.328 62.391 1.00 37.00 A ATOM 85 C ARG A 13 64.511 79.130 61.238 1.00 29.61 A ATOM 86 O ARG A 13 63.494 79.783 61.506 1.00 29.30 A ATOM 87 N PHE A 14 64.809 77.962 61.789 1.00 28.74 A ATOM 88 CA PHE A 14 63.980 77.337 62.797 1.00 28.90 A ATOM 89 CB PHE A 14 63.507 75.945 62.356 1.00 27.81 A ATOM 90 CG PHE A 14 62.614 75.946 61.147 1.00 26.25 A ATOM 91 CD1 PHE A 14 63.149 75.925 59.867 1.00 25.67 A ATOM 92 CD2 PHE A 14 61.235 75.955 61.291 1.00 27.94 A ATOM 93 CE1 PHE A 14 62.324 75.912 58.745 1.00 25.90 A ATOM 94 CE2 PHE A 14 60.393 75.942 60.174 1.00 27.89 A ATOM 95 CZ PHE A 14 60.940 75.921 58.896 1.00 26.23 A ATOM 96 C PHE A 14 64.847 77.185 64.032 1.00 30.32 A ATOM 97 O PHE A 14 66.004 76.760 63.959 1.00 30.71 A ATOM 98 N THR A 15 64.305 77.558 65.176 1.00 32.94 A ATOM 99 CA THR A 15 65.067 77.412 66.396 1.00 34.55 A ATOM 100 CB THR A 15 64.910 78.650 67.275 1.00 34.81 A ATOM 101 OG1 THR A 15 65.362 79.797 66.548 1.00 35.82 A ATOM 102 CG2 THR A 15 65.737 78.509 68.541 1.00 36.02 A ATOM 103 C THR A 15 64.535 76.179 67.119 1.00 34.29 A ATOM 104 O THR A 15 63.358 75.830 66.984 1.00 35.01 A ATOM 105 N VAL A 16 65.398 75.501 67.859 1.00 34.16 A ATOM 106 CA VAL A 16 64.954 74.330 68.592 1.00 36.47 A ATOM 107 CB VAL A 16 64.597 73.166 67.628 1.00 38.19 A ATOM 108 CG1 VAL A 16 65.697 72.981 66.579 1.00 37.94 A ATOM 109 CG2 VAL A 16 64.403 71.884 68.421 1.00 40.71 A ATOM 110 C VAL A 16 65.992 73.862 69.601 1.00 36.55 A ATOM 111 O VAL A 16 67.199 74.020 69.398 1.00 36.18 A ATOM 112 N ASP A 17 65.511 73.294 70.699 1.00 36.09 A ATOM 113 CA ASP A 17 66.398 72.817 71.750 1.00 36.61 A ATOM 114 CB ASP A 17 65.586 72.082 72.812 1.00 38.44 A ATOM 115 CG ASP A 17 66.458 71.416 73.840 1.00 40.95 A ATOM 116 OD1 ASP A 17 66.418 70.164 73.924 1.00 43.10 A ATOM 117 OD2 ASP A 17 67.184 72.137 74.556 1.00 41.69 A ATOM 118 C ASP A 17 67.499 71.902 71.196 1.00 35.77 A ATOM 119 O ASP A 17 67.218 70.903 70.543 1.00 33.05 A ATOM 120 N LYS A 18 68.757 72.245 71.471 1.00 36.17 A ATOM 121 CA LYS A 18 69.897 71.473 70.972 1.00 35.91 A ATOM 122 CB LYS A 18 71.208 72.003 71.541 1.00 35.90 A ATOM 123 CG LYS A 18 72.397 71.086 71.239 1.00 36.70 A ATOM 124 CD LYS A 18 73.679 71.525 71.964 1.00 37.63 A ATOM 125 CE LYS A 18 74.131 72.918 71.523 1.00 38.26 A ATOM 126 NZ LYS A 18 75.528 73.223 71.956 1.00 38.28 A ATOM 127 C LYS A 18 69.776 70.010 71.319 1.00 36.47 A ATOM 128 O LYS A 18 70.048 69.129 70.497 1.00 35.04 A ATOM 129 N LYS A 19 69.388 69.756 72.559 1.00 38.15 A ATOM 130 CA LYS A 19 69.220 68.393 73.011 1.00 38.79 A ATOM 131 CB LYS A 19 68.733 68.374 74.456 1.00 39.52 A ATOM 132 CG LYS A 19 68.597 66.980 75.018 0.00 40.07 A ATOM 133 CD LYS A 19 68.074 66.996 76.439 0.00 40.81 A ATOM 134 CE LYS A 19 66.638 67.489 76.505 0.00 41.30 A ATOM 135 NZ LYS A 19 66.086 67.373 77.885 0.00 41.65 A ATOM 136 C LYS A 19 68.202 67.734 72.084 1.00 38.59 A ATOM 137 O LYS A 19 68.508 66.734 71.445 1.00 39.10 A ATOM 138 N ILE A 20 67.004 68.304 71.984 1.00 37.46 A ATOM 139 CA ILE A 20 65.991 67.725 71.112 1.00 37.39 A ATOM 140 CB ILE A 20 64.685 68.503 71.168 1.00 36.72 A ATOM 141 CG2 ILE A 20 63.687 67.918 70.167 1.00 36.45 A ATOM 142 CG1 ILE A 20 64.118 68.440 72.572 1.00 35.02 A ATOM 143 CD1 ILE A 20 62.910 69.280 72.751 1.00 36.54 A ATOM 144 C ILE A 20 66.432 67.678 69.660 1.00 37.89 A ATOM 145 O ILE A 20 66.157 66.718 68.954 1.00 38.16 A ATOM 146 N ALA A 21 67.125 68.717 69.218 1.00 39.24 A ATOM 147 CA ALA A 21 67.591 68.793 67.843 1.00 38.28 A ATOM 148 CB ALA A 21 68.197 70.154 67.570 1.00 38.24 A ATOM 149 C ALA A 21 68.609 67.719 67.589 1.00 38.38 A ATOM 150 O ALA A 21 68.798 67.294 66.455 1.00 38.91 A ATOM 151 N GLU A 22 69.281 67.276 68.640 1.00 38.98 A ATOM 152 CA GLU A 22 70.280 66.242 68.449 1.00 39.28 A ATOM 153 CB GLU A 22 71.102 66.063 69.717 1.00 42.76 A ATOM 154 CG GLU A 22 72.116 67.162 69.962 1.00 47.53 A ATOM 155 CD GLU A 22 72.856 66.948 71.259 1.00 50.36 A ATOM 156 OE1 GLU A 22 73.381 65.827 71.444 1.00 50.70 A ATOM 157 OE2 GLU A 22 72.907 67.891 72.089 1.00 52.73 A ATOM 158 C GLU A 22 69.666 64.913 68.021 1.00 37.58 A ATOM 159 O GLU A 22 70.391 63.955 67.805 1.00 37.40 A ATOM 160 N ARG A 23 68.342 64.850 67.890 1.00 36.03 A ATOM 161 CA ARG A 23 67.706 63.615 67.459 1.00 34.62 A ATOM 162 CB ARG A 23 66.200 63.765 67.306 1.00 33.59 A ATOM 163 CG ARG A 23 65.509 62.431 67.022 1.00 33.69 A ATOM 164 CD ARG A 23 65.708 61.463 68.191 1.00 33.70 A ATOM 165 NE ARG A 23 64.457 61.196 68.901 1.00 34.45 A ATOM 166 CZ ARG A 23 64.360 60.622 70.100 1.00 33.77 A ATOM 167 NH1 ARG A 23 65.447 60.243 70.764 1.00 34.73 A ATOM 168 NH2 ARG A 23 63.164 60.414 70.633 1.00 29.73 A ATOM 169 C ARG A 23 68.270 63.248 66.116 1.00 35.80 A ATOM 170 O ARG A 23 68.362 62.077 65.769 1.00 37.71 A ATOM 171 N SER A 24 68.629 64.266 65.345 1.00 37.45 A ATOM 172 CA SER A 24 69.208 64.072 64.018 1.00 37.69 A ATOM 173 CB SER A 24 69.047 65.344 63.187 1.00 36.12 A ATOM 174 OG SER A 24 69.929 65.337 62.084 1.00 32.96 A ATOM 175 C SER A 24 70.686 63.729 64.127 1.00 38.12 A ATOM 176 O SER A 24 71.506 64.581 64.466 1.00 36.69 A ATOM 177 N LEU A 25 71.022 62.478 63.837 1.00 40.01 A ATOM 178 CA LEU A 25 72.409 62.036 63.901 1.00 42.65 A ATOM 179 CB LEU A 25 72.534 60.580 63.436 1.00 43.67 A ATOM 180 CG LEU A 25 71.996 59.493 64.383 1.00 43.11 A ATOM 181 CD1 LEU A 25 72.208 58.104 63.794 1.00 41.75 A ATOM 182 CD2 LEU A 25 72.703 59.615 65.713 1.00 41.72 A ATOM 183 C LEU A 25 73.313 62.916 63.054 1.00 42.76 A ATOM 184 O LEU A 25 74.475 63.112 63.394 1.00 42.58 A ATOM 185 N LEU A 26 72.779 63.442 61.954 1.00 44.29 A ATOM 186 CA LEU A 26 73.554 64.309 61.070 1.00 46.11 A ATOM 187 CB LEU A 26 72.701 64.742 59.875 1.00 46.16 A ATOM 188 CG LEU A 26 73.318 65.721 58.868 1.00 45.56 A ATOM 189 CD1 LED A 26 74.571 65.123 58.268 1.00 44.90 A ATOM 190 CD2 LED A 26 72.303 66.050 57.774 1.00 45.90 A ATOM 191 C LED A 26 73.992 65.524 61.866 1.00 47.66 A ATOM 192 O LED A 26 75.140 65.962 61.770 1.00 47.34 A ATOM 193 N LEU A 27 73.060 66.055 62.655 1.00 50.27 A ATOM 194 CA LED A 27 73.312 67.212 63.508 1.00 52.62 A ATOM 195 CB LEU A 27 71.985 67.831 63.963 1.00 52.60 A ATOM 196 CG LED A 27 72.112 68.911 65.046 1.00 52.80 A ATOM 197 CD1 LEU A 27 72.872 70.114 64.501 1.00 52.04 A ATOM 198 CD2 LED A 27 70.729 69.314 65.513 1.00 52.96 A ATOM 199 C LED A 27 74.145 66.835 64.742 1.00 54.44 A ATOM 200 O LED A 27 75.085 67.540 65.100 1.00 54.34 A ATOM 201 N LYS A 28 73.786 65.726 65.387 1.00 56.05 A ATOM 202 CA LYS A 28 74.491 65.255 66.574 1.00 57.53 A ATOM 203 CB LYS A 28 73.880 63.942 67.059 1.00 58.27 A ATOM 204 CG LYS A 28 74.486 63.418 68.347 0.00 58.77 A ATOM 205 CD LYS A 28 73.864 62.093 68.750 0.00 59.35 A ATOM 206 CE LYS A 28 74.520 61.545 70.004 0.00 59.70 A ATOM 207 NZ LYS A 28 73.986 60.205 70.367 0.00 59.95 A ATOM 208 C LYS A 28 75.974 65.049 66.297 0.00 58.99 A ATOM 209 O LYS A 28 76.811 65.183 67.191 0.00 58.95 A ATOM 210 N ASN A 29 76.290 64.716 65.052 1.00 60.36 A ATOM 211 CA ASN A 29 77.667 64.489 64.647 1.00 62.38 A ATOM 212 CB ASN A 29 77.729 63.509 63.484 1.00 63.15 A ATOM 213 CG ASN A 29 77.458 62.085 63.908 1.00 64.88 A ATOM 214 OD1 ASN A 29 77.410 61.185 63.068 1.00 67.16 A ATOM 215 ND2 ASN A 29 77.285 61.865 65.215 1.00 64.20 A ATOM 216 C ASN A 29 78.326 65.778 64.227 1.00 63.19 A ATOM 217 O ASN A 29 79.547 65.852 64.106 1.00 63.26 A ATOM 218 N TYR A 30 77.514 66.797 63.993 1.00 64.46 A ATOM 219 CA TYR A 30 78.049 68.083 63.583 1.00 65.53 A ATOM 220 CB TYR A 30 76.898 69.085 63.417 1.00 67.82 A ATOM 221 CG TYR A 30 77.127 70.172 62.379 1.00 68.70 A ATOM 222 CD1 TYR A 30 77.416 69.853 61.050 1.00 68.47 A ATOM 223 CE1 TYR A 30 77.595 70.854 60.092 1.00 69.31 A ATOM 224 CD2 TYR A 30 77.024 71.522 62.722 1.00 68.53 A ATOM 225 CE2 TYR A 30 77.201 72.528 61.774 1.00 69.17 A ATOM 226 CZ TYR A 30 77.485 72.190 60.464 1.00 69.54 A ATOM 227 OH TYR A 30 77.651 73.191 59.534 1.00 69.67 A ATOM 228 C TYR A 30 79.043 68.550 64.658 1.00 65.21 A ATOM 229 O TYR A 30 79.894 69.395 64.391 1.00 64.91 A ATOM 230 N VAL A 31 78.935 67.964 65.856 1.00 64.85 A ATOM 231 CA VAL A 31 79.786 68.271 67.019 1.00 62.98 A ATOM 232 CB VAL A 31 81.049 67.351 67.096 1.00 62.18 A ATOM 233 CG1 VAL A 31 80.624 65.903 67.216 1.00 61.36 A ATOM 234 CG2 VAL A 31 81.961 67.562 65.882 1.00 60.58 A ATOM 235 C VAL A 31 80.256 69.712 67.123 1.00 62.08 A ATOM 236 O VAL A 31 80.624 70.168 68.203 1.00 60.74 A ATOM 237 N ILE A 45 76.524 76.394 65.711 1.00 42.05 A ATOM 238 CA ILE A 45 75.216 76.668 66.290 1.00 41.90 A ATOM 239 CB ILE A 45 75.276 77.864 67.310 1.00 42.05 A ATOM 240 CG2 ILE A 45 75.089 79.191 66.601 1.00 40.06 A ATOM 241 CG1 ILE A 45 74.171 77.726 68.363 1.00 43.22 A ATOM 242 CD1 ILE A 45 74.407 76.620 69.388 1.00 43.84 A ATOM 243 C ILE A 45 74.180 76.963 65.195 1.00 41.36 A ATOM 244 O ILE A 45 73.021 77.252 65.488 1.00 41.48 A ATOM 245 N VAL A 46 74.592 76.918 63.933 1.00 39.64 A ATOM 246 CA VAL A 46 73.635 77.132 62.849 1.00 39.19 A ATOM 247 CB VAL A 46 73.675 78.579 62.293 1.00 37.60 A ATOM 248 CG1 VAL A 46 72.665 78.729 61.166 1.00 35.40 A ATOM 249 CG2 VAL A 46 73.346 79.567 63.390 1.00 38.18 A ATOM 250 C VAL A 46 73.917 76.159 61.715 1.00 39.41 A ATOM 251 O VAL A 46 74.815 76.385 60.905 1.00 41.28 A ATOM 252 N MSE A 47 73.160 75.069 61.655 1.00 38.13 A ATOM 253 CA MSE A 47 73.390 74.093 60.606 1.00 37.60 A ATOM 254 CB MSE A 47 73.419 72.680 61.169 1.00 40.79 A ATOM 255 CG MSE A 47 73.777 71.642 60.118 1.00 44.02 A ATOM 256 SE MSE A 47 73.314 69.875 60.679 1.00 50.37 A ATOM 257 CE MSE A 47 71.388 70.111 60.653 1.00 48.04 A ATOM 258 C MSE A 47 72.402 74.138 59.465 1.00 36.07 A ATOM 259 O MSE A 47 71.195 74.213 59.670 1.00 36.45 A ATOM 260 N PRO A 48 72.917 74.093 58.229 1.00 34.97 A ATOM 261 CD PRO A 48 74.305 74.434 57.870 1.00 34.19 A ATOM 262 CA PRO A 48 72.066 74.128 57.040 1.00 34.14 A ATOM 263 CB PRO A 48 73.041 74.516 55.929 1.00 33.07 A ATOM 264 CG PRO A 48 74.103 75.290 56.654 1.00 33.93 A ATOM 265 C PRO A 48 71.369 72.806 56.729 1.00 33.52 A ATOM 266 O PRO A 48 71.922 71.727 56.946 1.00 32.95 A ATOM 267 N VAL A 49 70.140 72.906 56.231 1.00 32.78 A ATOM 268 CA VAL A 49 69.383 71.731 55.828 1.00 32.43 A ATOM 269 CB VAL A 49 68.073 71.538 56.671 1.00 31.33 A ATOM 270 CG1 VAL A 49 67.575 70.120 56.539 1.00 30.50 A ATOM 271 CG2 VAL A 49 68.327 71.845 58.141 1.00 34.13 A ATOM 272 C VAL A 49 69.062 71.991 54.340 1.00 32.95 A ATOM 273 O VAL A 49 67.958 72.412 53.977 1.00 32.24 A ATOM 274 N PRO A 50 70.060 71.757 53.460 1.00 33.40 A ATOM 275 CD PRO A 50 71.393 71.237 53.811 1.00 33.34 A ATOM 276 CA PRO A 50 69.971 71.942 52.010 1.00 32.39 A ATOM 277 CB PRO A 50 71.310 71.409 51.512 1.00 32.52 A ATOM 278 CG PRO A 50 72.217 71.682 52.627 1.00 33.15 A ATOM 279 C PRO A 50 68.813 71.229 51.343 1.00 31.05 A ATOM 280 O PRO A 50 68.509 70.079 51.648 1.00 31.50 A ATOM 281 N ASN A 51 68.176 71.936 50.420 1.00 30.37 A ATOM 282 CA ASN A 51 67.071 71.387 49.645 1.00 30.66 A ATOM 283 CB ASN A 51 67.648 70.432 48.595 1.00 31.76 A ATOM 284 CG ASN A 51 69.069 70.813 48.175 1.00 30.85 A ATOM 285 OD1 ASN A 51 69.262 71.794 47.478 1.00 27.98 A ATOM 286 ND2 ASN A 51 70.072 70.031 48.620 1.00 33.14 A ATOM 287 C ASN A 51 65.978 70.665 50.450 1.00 29.20 A ATOM 288 O ASN A 51 65.588 69.551 50.120 1.00 26.62 A ATOM 289 N VAL A 52 65.500 71.292 51.512 1.00 29.33 A ATOM 290 CA VAL A 52 64.435 70.692 52.283 1.00 29.38 A ATOM 291 CB VAL A 52 64.913 70.157 53.640 1.00 30.20 A ATOM 292 CG1 VAL A 52 63.747 69.506 54.390 1.00 26.29 A ATOM 293 CG2 VAL A 52 66.022 69.129 53.420 1.00 29.10 A ATOM 294 C VAL A 52 63.401 71.774 52.492 1.00 29.83 A ATOM 295 O VAL A 52 63.693 72.821 53.058 1.00 29.62 A ATOM 296 N ARG A 53 62.199 71.504 51.992 1.00 30.70 A ATOM 297 CA ARG A 53 61.064 72.411 52.063 1.00 31.16 A ATOM 298 CB ARG A 53 59.814 71.667 51.580 1.00 35.30 A ATOM 299 CG ARG A 53 58.775 72.499 50.846 1.00 39.79 A ATOM 300 CD ARG A 53 57.564 71.636 50.474 1.00 42.92 A ATOM 301 NE ARG A 53 56.700 72.283 49.491 1.00 47.91 A ATOM 302 CZ ARG A 53 55.889 73.308 49.749 1.00 50.95 A ATOM 303 NH1 ARG A 53 55.815 73.814 50.972 1.00 53.87 A ATOM 304 NH2 ARC A 53 55.158 73.844 48.776 1.00 52.85 A ATOM 305 C ARC A 53 60.864 72.876 53.505 1.00 30.38 A ATOM 306 O ARC A 53 60.860 72.068 54.425 1.00 31.84 A ATOM 307 N SER A 54 60.694 74.173 53.708 1.00 27.65 A ATOM 308 CA SER A 54 60.481 74.670 55.050 1.00 24.25 A ATOM 309 CB SER A 54 60.094 76.142 55.013 1.00 23.48 A ATOM 310 OC SER A 54 61.197 76.935 54.642 1.00 22.07 A ATOM 311 C SER A 54 59.386 73.866 55.742 1.00 22.74 A ATOM 312 O SER A 54 59.611 73.280 56.792 1.00 21.74 A ATOM 313 N SER A 55 58.204 73.835 55.143 1.00 22.72 A ATOM 314 CA SER A 55 57.078 73.114 55.707 1.00 22.82 A ATOM 315 CB SER A 55 55.913 73.117 54.736 1.00 20.88 A ATOM 316 OC SER A 55 56.159 72.211 53.683 1.00 23.15 A ATOM 317 C SER A 55 57.432 71.670 56.042 1.00 24.40 A ATOM 318 O SER A 55 56.780 71.034 56.877 1.00 27.21 A ATOM 319 N VAL A 56 58.457 71.144 55.387 1.00 21.45 A ATOM 320 CA VAL A 56 58.862 69.782 55.662 1.00 20.79 A ATOM 321 CB VAL A 56 59.648 69.194 54.488 1.00 19.14 A ATOM 322 CG1 VAL A 56 60.254 67.875 54.889 1.00 16.99 A ATOM 323 CG2 VAL A 56 58.738 69.029 53.301 1.00 18.04 A ATOM 324 C VAL A 56 59.719 69.727 56.924 1.00 21.47 A ATOM 325 O VAL A 56 59.498 68.903 57.797 1.00 21.73 A ATOM 326 N LEU A 57 60.703 70.606 57.010 1.00 22.90 A ATOM 327 CA LEU A 57 61.573 70.645 58.159 1.00 24.53 A ATOM 328 CB LEU A 57 62.647 71.696 57.937 1.00 24.08 A ATOM 329 CG LEU A 57 63.681 71.859 59.042 1.00 24.59 A ATOM 330 CD1 LEU A 57 64.030 70.523 59.664 1.00 23.09 A ATOM 331 CD2 LEU A 57 64.924 72.530 58.438 1.00 23.83 A ATOM 332 C LEU A 57 60.760 70.949 59.411 1.00 27.00 A ATOM 333 O LEU A 57 61.044 70.424 60.486 1.00 27.31 A ATOM 334 N GLN A 58 59.740 71.790 59.270 1.00 28.60 A ATOM 335 CA GLN A 58 58.885 72.133 60.402 1.00 29.92 A ATOM 336 CB GLN A 58 57.789 73.112 59.979 1.00 29.50 A ATOM 337 CG GLN A 58 56.729 73.358 61.044 1.00 29.08 A ATOM 338 CD GLN A 58 55.975 74.654 60.815 1.00 27.90 A ATOM 339 OE1 GLN A 58 56.591 75.700 60.657 1.00 30.17 A ATOM 340 NE2 GLN A 58 54.648 74.594 60.802 1.00 25.55 A ATOM 341 C GLN A 58 58.257 70.845 60.886 1.00 30.93 A ATOM 342 O GLN A 58 58.354 70.483 62.065 1.00 33.35 A ATOM 343 N LYS A 59 57.609 70.156 59.955 1.00 30.29 A ATOM 344 CA LYS A 59 56.976 68.880 60.248 1.00 29.48 A ATOM 345 CB LYS A 59 56.581 68.209 58.937 1.00 28.21 A ATOM 346 CG LYS A 59 55.283 67.470 58.978 1.00 29.03 A ATOM 347 CD LYS A 59 54.108 68.397 59.081 1.00 27.32 A ATOM 348 CE LYS A 59 52.834 67.608 58.857 1.00 26.80 A ATOM 349 NZ LYS A 59 52.804 66.508 59.824 1.00 25.00 A ATOM 350 C LYS A 59 58.004 68.017 61.006 1.00 29.46 A ATOM 351 O LYS A 59 57.709 67.465 62.070 1.00 29.02 A ATOM 352 N VAL A 60 59.217 67.929 60.467 1.00 28.15 A ATOM 353 CA VAL A 60 60.259 67.142 61.106 1.00 28.14 A ATOM 354 CB VAL A 60 61.573 67.226 60.319 1.00 28.15 A ATOM 355 CG1 VAL A 60 62.731 66.715 61.152 1.00 27.46 A ATOM 356 CG2 VAL A 60 61.455 66.386 59.060 1.00 29.05 A ATOM 357 C VAL A 60 60.495 67.574 62.543 1.00 28.57 A ATOM 358 O VAL A 60 60.434 66.762 63.465 1.00 29.28 A ATOM 359 N ILE A 61 60.768 68.853 62.734 1.00 28.79 A ATOM 360 CA ILE A 61 61.007 69.375 64.068 1.00 28.54 A ATOM 361 CB ILE A 61 61.195 70.903 64.001 1.00 27.31 A ATOM 362 CG2 ILE A 61 61.238 71.501 65.391 1.00 26.36 A ATOM 363 CG1 ILE A 61 62.482 71.202 63.223 1.00 27.68 A ATOM 364 CD1 ILE A 61 62.737 72.660 62.979 1.00 27.54 A ATOM 365 C ILE A 61 59.860 69.020 65.016 1.00 29.35 A ATOM 366 O ILE A 61 60.086 68.538 66.131 1.00 27.58 A ATOM 367 N GLU A 62 58.627 69.247 64.572 1.00 30.00 A ATOM 368 CA GLU A 62 57.473 68.949 65.415 1.00 31.73 A ATOM 369 CB GLU A 62 56.169 69.203 64.667 1.00 29.92 A ATOM 370 CG GLU A 62 55.043 68.328 65.181 1.00 30.57 A ATOM 371 CD GLU A 62 53.688 68.775 64.703 1.00 31.86 A ATOM 372 OE1 GLU A 62 53.530 68.966 63.470 1.00 33.09 A ATOM 373 OE2 GLU A 62 52.781 68.934 65.562 1.00 31.63 A ATOM 374 C GLU A 62 57.480 67.505 65.907 1.00 32.78 A ATOM 375 O GLU A 62 57.035 67.207 67.017 1.00 32.73 A ATOM 376 N TRP A 63 57.965 66.610 65.057 1.00 34.15 A ATOM 377 CA TRP A 63 58.029 65.204 65.394 1.00 34.37 A ATOM 378 CB TRP A 63 58.259 64.380 64.127 1.00 33.74 A ATOM 379 CG TRP A 63 58.189 62.915 64.354 1.00 31.94 A ATOM 380 CD2 TRP A 63 59.254 62.071 64.798 1.00 30.34 A ATOM 381 CE2 TRP A 63 58.729 60.775 64.937 1.00 29.79 A ATOM 382 CE3 TRP A 63 60.601 62.287 65.104 1.00 29.39 A ATOM 383 CD1 TRP A 63 57.092 62.120 64.235 1.00 31.15 A ATOM 384 NE1 TRP A 63 57.406 60.829 64.584 1.00 30.29 A ATOM 385 CZ2 TRP A 63 59.506 59.698 65.361 1.00 29.60 A ATOM 386 CZ3 TRP A 63 61.372 61.211 65.528 1.00 28.85 A ATOM 387 CH2 TRP A 63 60.821 59.937 65.654 1.00 27.95 A ATOM 388 C TRP A 63 59.181 64.989 66.372 1.00 34.92 A ATOM 389 O TRP A 63 59.146 64.078 67.182 1.00 36.00 A ATOM 390 N ALA A 64 60.195 65.840 66.316 1.00 35.06 A ATOM 391 CA ALA A 64 61.332 65.673 67.207 1.00 36.52 A ATOM 392 CB ALA A 64 62.567 66.371 66.621 1.00 35.61 A ATOM 393 C ALA A 64 61.071 66.166 68.636 1.00 38.06 A ATOM 394 O ALA A 64 61.606 65.607 69.602 1.00 38.15 A ATOM 395 N GLU A 65 60.266 67.218 68.764 1.00 38.68 A ATOM 396 CA GLU A 65 59.934 67.776 70.063 1.00 38.24 A ATOM 397 CB GLU A 65 59.405 69.201 69.912 1.00 38.18 A ATOM 398 CG GLU A 65 60.459 70.151 69.397 1.00 38.80 A ATOM 399 CD GLU A 65 59.895 71.454 68.840 1.00 39.78 A ATOM 400 OE1 GLU A 65 58.673 71.527 68.547 1.00 38.29 A ATOM 401 OE2 GLU A 65 60.695 72.408 68.683 1.00 39.80 A ATOM 402 C GLU A 65 58.879 66.902 70.708 1.00 38.37 A ATOM 403 O GLU A 65 58.835 66.742 71.925 1.00 39.26 A ATOM 404 N HIS A 66 58.024 66.312 69.896 1.00 38.38 A ATOM 405 CA HIS A 66 57.006 65.482 70.479 1.00 40.16 A ATOM 406 CB HIS A 66 55.929 65.179 69.465 1.00 39.56 A ATOM 407 CG HIS A 66 54.902 64.215 69.955 1.00 39.86 A ATOM 408 CD2 HIS A 66 53.613 64.399 70.320 1.00 39.39 A ATOM 409 ND1 HIS A 66 55.137 62.859 70.036 1.00 38.45 A ATOM 410 CE1 HIS A 66 54.031 62.248 70.418 1.00 38.21 A ATOM 411 NE2 HIS A 66 53.091 63.159 70.595 1.00 39.69 A ATOM 412 C HIS A 66 57.616 64.205 71.002 1.00 42.15 A ATOM 413 O HIS A 66 57.115 63.619 71.959 1.00 44.74 A ATOM 414 N HIS A 67 58.701 63.775 70.377 1.00 43.11 A ATOM 415 CA HIS A 67 59.388 62.573 70.807 1.00 44.64 A ATOM 416 CB HIS A 67 59.711 61.681 69.598 1.00 43.57 A ATOM 417 CG HIS A 67 58.524 60.951 69.046 1.00 42.88 A ATOM 418 CD2 HIS A 67 58.088 59.684 69.241 1.00 42.35 A ATOM 419 ND1 HIS A 67 57.615 61.540 68.194 1.00 43.39 A ATOM 420 CE1 HIS A 67 56.673 60.667 67.886 1.00 41.93 A ATOM 421 NE2 HIS A 67 56.936 59.533 68.508 1.00 40.92 A ATOM 422 C HIS A 67 60.673 62.989 71.512 1.00 46.18 A ATOM 423 O HIS A 67 61.767 62.552 71.144 1.00 47.55 A ATOM 424 N ARG A 68 60.541 63.842 72.524 1.00 47.19 A ATOM 425 CA ARG A 68 61.704 64.322 73.270 1.00 48.05 A ATOM 426 CB ARG A 68 61.390 65.665 73.959 1.00 47.55 A ATOM 427 CG ARG A 68 60.459 65.576 75.163 1.00 47.12 A ATOM 428 CD ARG A 68 60.219 66.943 75.813 1.00 45.40 A ATOM 429 NE ARG A 68 59.137 67.657 75.151 1.00 44.72 A ATOM 430 CZ ARG A 68 57.849 67.387 75.342 1.00 44.29 A ATOM 431 NH1 ARG A 68 57.485 66.434 76.179 1.00 46.93 A ATOM 432 NH2 ARG A 68 56.915 68.043 74.678 1.00 45.61 A ATOM 433 C ARG A 68 62.187 63.308 74.303 1.00 49.19 A ATOM 434 O ARG A 68 63.383 63.228 74.593 1.00 48.48 A ATOM 435 N ASP A 69 61.261 62.525 74.848 1.00 51.12 A ATOM 436 CA ASP A 69 61.626 61.531 75.853 1.00 52.05 A ATOM 437 CB ASP A 69 60.967 61.862 77.187 1.00 50.12 A ATOM 438 CG ASP A 69 61.351 63.221 77.684 1.00 49.36 A ATOM 439 OD1 ASP A 69 62.572 63.496 77.736 1.00 48.50 A ATOM 440 OD2 ASP A 69 60.440 64.010 78.015 1.00 49.39 A ATOM 441 C ASP A 69 61.245 60.126 75.442 1.00 52.86 A ATOM 442 O ASP A 69 60.787 59.335 76.261 1.00 52.94 A ATOM 443 N SER A 70 61.437 59.812 74.170 1.00 54.02 A ATOM 444 CA SER A 70 61.106 58.488 73.690 1.00 55.97 A ATOM 445 CB SER A 70 60.259 58.588 72.425 1.00 54.70 A ATOM 446 OG SER A 70 59.031 59.239 72.703 1.00 54.60 A ATOM 447 C SER A 70 62.379 57.702 73.425 1.00 58.22 A ATOM 448 O SER A 70 63.463 58.273 73.306 1.00 58.71 A ATOM 449 N ASN A 71 62.252 56.385 73.362 1.00 60.80 A ATOM 450 CA ASN A 71 63.403 55.545 73.105 1.00 64.11 A ATOM 451 CB ASN A 71 63.999 55.049 74.421 1.00 62.74 A ATOM 452 CG ASN A 71 64.012 56.121 75.495 1.00 62.42 A ATOM 453 OD1 ASN A 71 63.016 56.332 76.183 1.00 61.70 A ATOM 454 ND2 ASN A 71 65.139 56.811 75.636 1.00 62.41 A ATOM 455 C ASN A 71 62.957 54.377 72.247 1.00 67.50 A ATOM 456 O ASN A 71 62.140 53.558 72.669 1.00 68.91 A ATOM 457 N PHE A 72 63.486 54.313 71.030 1.00 70.54 A ATOM 458 CA PHE A 72 63.134 53.245 70.110 1.00 72.15 A ATOM 459 CB PHE A 72 62.792 53.827 68.721 1.00 72.15 A ATOM 460 CG PHE A 72 61.940 55.087 68.759 1.00 71.12 A ATOM 461 CD1 PHE A 72 62.539 56.349 68.784 1.00 70.74 A ATOM 462 CD2 PHE A 72 60.546 55.012 68.765 1.00 70.32 A ATOM 463 CE1 PHE A 72 61.767 57.514 68.814 1.00 70.31 A ATOM 464 CE2 PHE A 72 59.768 56.173 68.796 1.00 70.64 A ATOM 465 CZ PHE A 72 60.383 57.425 68.821 1.00 70.21 A ATOM 466 C PHE A 72 64.307 52.261 70.001 1.00 73.60 A ATOM 467 O PHE A 72 65.466 52.623 70.226 1.00 73.93 A ATOM 468 N PRO A 73 64.012 50.992 69.685 1.00 75.25 A ATOM 469 CD PRO A 73 62.656 50.410 69.635 1.00 75.90 A ATOM 470 CA PRO A 73 65.039 49.952 69.545 1.00 75.83 A ATOM 471 CB PRO A 73 64.230 48.732 69.122 1.00 76.63 A ATOM 472 CG PRO A 73 62.924 48.937 69.852 1.00 76.34 A ATOM 473 C PRO A 73 66.099 50.325 68.511 0.00 76.16 A ATOM 474 O PRO A 73 67.292 50.365 68.813 0.00 76.37 A ATOM 475 N VAL A 86 52.596 52.678 63.351 1.00 68.06 A ATOM 476 CA VAL A 86 52.119 51.882 64.474 1.00 69.23 A ATOM 477 CB VAL A 86 53.259 50.998 65.073 1.00 69.13 A ATOM 478 CG1 VAL A 86 52.716 50.130 66.203 1.00 68.76 A ATOM 479 CG2 VAL A 86 53.864 50.111 63.989 1.00 69.85 A ATOM 480 C VAL A 86 51.576 52.809 65.562 1.00 69.62 A ATOM 481 O VAL A 86 50.459 52.627 66.061 1.00 69.53 A ATOM 482 N ASP A 87 52.368 53.821 65.907 1.00 69.73 A ATOM 483 CA ASP A 87 51.995 54.792 66.936 1.00 68.97 A ATOM 484 CB ASP A 87 53.177 55.726 67.223 1.00 70.05 A ATOM 485 CG ASP A 87 52.982 56.555 68.487 1.00 70.55 A ATOM 486 OD1 ASP A 87 52.047 57.386 68.514 1.00 70.97 A ATOM 487 OD2 ASP A 87 53.768 56.374 69.447 1.00 69.47 A ATOM 488 C ASP A 87 50.766 55.609 66.528 1.00 67.85 A ATOM 489 O ASP A 87 50.574 55.925 65.353 1.00 67.51 A ATOM 490 N SER A 88 49.936 55.948 67.510 1.00 66.47 A ATOM 491 CA SER A 88 48.714 56.708 67.263 1.00 64.69 A ATOM 492 CB SER A 88 47.872 56.772 68.537 1.00 65.29 A ATOM 493 OG SER A 88 46.724 57.579 68.337 1.00 66.37 A ATOM 494 C SER A 88 48.976 58.124 66.770 1.00 62.66 A ATOM 495 O SER A 88 48.420 58.553 65.755 1.00 61.70 A ATOM 496 N TRP A 89 49.824 58.843 67.498 1.00 60.57 A ATOM 497 CA TRP A 89 50.161 60.221 67.160 1.00 58.68 A ATOM 498 CB TRP A 89 50.999 60.836 68.281 1.00 57.33 A ATOM 499 CG TRP A 89 51.130 62.296 68.148 1.00 56.37 A ATOM 500 CD2 TRP A 89 52.229 62.998 67.571 1.00 56.15 A ATOM 501 CE2 TRP A 89 51.892 64.365 67.574 1.00 55.64 A ATOM 502 CE3 TRP A 89 53.463 62.605 67.044 1.00 55.77 A ATOM 503 CD1 TRP A 89 50.201 63.231 68.477 1.00 54.82 A ATOM 504 NE1 TRP A 89 50.649 64.480 68.136 1.00 54.93 A ATOM 505 CZ2 TRP A 89 52.755 65.342 67.072 1.00 55.82 A ATOM 506 CZ3 TRP A 89 54.315 63.579 66.544 1.00 55.23 A ATOM 507 CH2 TRP A 89 53.957 64.927 66.561 1.00 55.54 A ATOM 508 C TRP A 89 50.915 60.332 65.831 1.00 57.32 A ATOM 509 O TRP A 89 50.679 61.248 65.045 1.00 57.65 A ATOM 510 NA SP A 90 51.827 59.398 65.593 1.00 55.46 A ATOM 511 CA ASP A 90 52.602 59.387 64.366 1.00 53.21 A ATOM 512 CB ASP A 90 53.710 58.353 64.472 1.00 51.45 A ATOM 513 CG ASP A 90 54.795 58.795 65.396 1.00 51.44 A ATOM 514 OD1 ASP A 90 54.462 59.439 66.401 1.00 53.33 A ATOM 515 OD2 ASP A 90 55.975 58.511 65.134 1.00 51.16 A ATOM 516 C ASP A 90 51.731 59.082 63.162 1.00 53.01 A ATOM 517 O ASP A 90 51.943 59.625 62.076 1.00 53.15 A ATOM 518 N ARG A 91 50.746 58.214 63.362 1.00 52.99 A ATOM 519 CA ARG A 91 49.835 57.822 62.293 1.00 52.82 A ATOM 520 CB ARG A 91 48.865 56.747 62.802 1.00 53.81 A ATOM 521 CG ARG A 91 47.856 56.264 61.770 1.00 56.18 A ATOM 522 CD ARG A 91 47.412 54.828 62.031 1.00 58.29 A ATOM 523 NE ARG A 91 46.995 54.617 63.412 1.00 61.35 A ATOM 524 CZ ARG A 91 45.922 55.168 63.972 1.00 62.36 A ATOM 525 NH1 ARG A 91 45.138 55.972 63.267 1.00 64.03 A ATOM 526 NH2 ARG A 91 45.640 54.925 65.246 1.00 63.29 A ATOM 527 C ARG A 91 49.065 59.014 61.728 1.00 51.91 A ATOM 528 O ARG A 91 48.829 59.086 60.522 1.00 51.24 A ATOM 529 N GLU A 92 48.683 59.946 62.599 1.00 50.83 A ATOM 530 CA GLU A 92 47.955 61.136 62.172 1.00 50.40 A ATOM 531 CB GLU A 92 47.181 61.750 63.337 1.00 52.44 A ATOM 532 CG GLU A 92 46.026 60.914 63.856 1.00 58.05 A ATOM 533 CD GLU A 92 44.989 60.594 62.787 1.00 60.95 A ATOM 534 OE1 GLU A 92 44.493 61.541 62.125 1.00 61.85 A ATOM 535 OE2 GLU A 92 44.670 59.392 62.621 1.00 61.47 A ATOM 536 C GLU A 92 48.929 62.174 61.632 1.00 48.17 A ATOM 537 O GLU A 92 48.689 62.784 60.589 1.00 48.86 A ATOM 538 N PHE A 93 50.020 62.376 62.364 1.00 45.11 A ATOM 539 CA PHE A 93 51.056 63.325 61.989 1.00 42.22 A ATOM 540 CB PHE A 93 52.241 63.197 62.930 1.00 39.86 A ATOM 541 CG PHE A 93 53.473 63.881 62.431 1.00 38.61 A ATOM 542 CD1 PHE A 93 53.560 65.270 62.434 1.00 38.78 A ATOM 543 CD2 PHE A 93 54.550 63.139 61.949 1.00 38.41 A ATOM 544 CE1 PHE A 93 54.706 65.920 61.962 1.00 37.98 A ATOM 545 CE2 PHE A 93 55.702 63.771 61.474 1.00 37.53 A ATOM 546 CZ PHE A 93 55.782 65.169 61.482 1.00 37.66 A ATOM 547 C PHE A 93 51.529 63.039 60.586 1.00 41.92 A ATOM 548 O PHE A 93 51.915 63.940 59.847 1.00 42.62 A ATOM 549 N LEU A 94 51.513 61.766 60.229 1.00 41.18 A ATOM 550 CA LEU A 94 51.938 61.368 58.913 1.00 40.65 A ATOM 551 CB LEU A 94 52.602 60.008 58.986 1.00 39.81 A ATOM 552 CG LEU A 94 53.987 60.082 59.611 1.00 40.12 A ATOM 553 CD1 LEU A 94 54.560 58.682 59.692 1.00 40.00 A ATOM 554 CD2 LEU A 94 54.889 60.998 58.785 1.00 38.29 A ATOM 555 C LEU A 94 50.792 61.333 57.927 1.00 41.17 A ATOM 556 O LEU A 94 51.010 61.120 56.737 1.00 41.27 A ATOM 557 N LYS A 95 49.575 61.553 58.413 1.00 41.25 A ATOM 558 CA LYS A 95 48.420 61.534 57.532 1.00 42.22 A ATOM 559 CB LYS A 95 47.120 61.460 58.342 1.00 43.14 A ATOM 560 CG LYS A 95 45.925 61.168 57.438 1.00 47.48 A ATOM 561 CD LYS A 95 44.586 61.331 58.138 1.00 51.30 A ATOM 562 CE LYS A 95 44.392 60.305 59.252 1.00 53.68 A ATOM 563 NZ LYS A 95 43.042 60.431 59.895 1.00 54.53 A ATOM 564 C LYS A 95 48.390 62.762 56.616 1.00 41.83 A ATOM 565 O LYS A 95 47.450 63.552 56.650 1.00 42.87 A ATOM 566 N VAL A 96 49.406 62.890 55.770 1.00 41.34 A ATOM 567 CA VAL A 96 49.545 64.023 54.856 1.00 40.71 A ATOM 568 CB VAL A 96 50.909 64.673 55.057 1.00 40.36 A ATOM 569 CG1 VAL A 96 51.034 65.180 56.471 1.00 39.98 A ATOM 570 CG2 VAL A 96 51.990 63.651 54.777 1.00 38.65 A ATOM 571 C VAL A 96 49.446 63.611 53.385 1.00 41.10 A ATOM 572 O VAL A 96 49.074 62.482 53.077 1.00 39.99 A ATOM 573 N ASP A 97 49.789 64.518 52.471 1.00 41.74 A ATOM 574 CA ASP A 97 49.729 64.155 51.064 1.00 43.35 A ATOM 575 CB ASP A 97 49.500 65.386 50.168 1.00 46.03 A ATOM 576 CG ASP A 97 50.694 66.307 50.088 1.00 49.27 A ATOM 577 OD1 ASP A 97 51.762 65.862 49.621 1.00 51.92 A ATOM 578 OD2 ASP A 97 50.560 67.490 50.476 1.00 50.75 A ATOM 579 C ASP A 97 50.976 63.369 50.642 1.00 42.71 A ATOM 580 O ASP A 97 52.039 63.493 51.249 1.00 42.39 A ATOM 581 N GLN A 98 50.815 62.549 49.606 1.00 41.92 A ATOM 582 CA GLN A 98 51.867 61.690 49.097 1.00 40.58 A ATOM 583 CB GLN A 98 51.392 60.988 47.807 1.00 42.66 A ATOM 584 CG GLN A 98 49.949 60.414 47.882 1.00 43.12 A ATOM 585 CD GLN A 98 49.666 59.270 46.905 1.00 43.62 A ATOM 586 OE1 CLN A 98 48.516 58.876 46.720 1.00 42.97 A ATOM 587 NE2 GLN A 98 50.712 58.732 46.290 1.00 44.27 A ATOM 588 C GLN A 98 53.173 62.428 48.870 1.00 39.89 A ATOM 589 O GLN A 98 54.234 61.905 49.180 1.00 38.30 A ATOM 590 N GLU A 99 53.114 63.640 48.330 1.00 40.88 A ATOM 591 CA GLU A 99 54.343 64.404 48.118 1.00 40.74 A ATOM 592 CB GLU A 99 54.035 65.695 47.377 1.00 41.69 A ATOM 593 CG GLU A 99 53.880 65.494 45.903 1.00 47.00 A ATOM 594 CD GLU A 99 55.182 65.074 45.254 1.00 48.98 A ATOM 595 OE1 GLU A 99 56.236 65.569 45.721 1.00 50.30 A ATOM 596 OE2 GLU A 99 55.154 64.274 44.284 1.00 48.68 A ATOM 597 C GLU A 99 54.984 64.710 49.474 1.00 39.87 A ATOM 598 O GLU A 99 56.164 64.426 49.691 1.00 39.94 A ATOM 599 N MSE A 100 54.187 65.272 50.382 1.00 39.05 A ATOM 600 CA MSE A 100 54.637 65.617 51.729 1.00 39.03 A ATOM 601 CB MSE A 100 53.434 66.000 52.603 1.00 45.07 A ATOM 602 CG MSE A 100 53.726 66.188 54.093 1.00 50.78 A ATOM 603 SE MSE A 100 54.480 67.900 54.500 1.00 61.41 A ATOM 604 CE MSE A 100 56.351 67.467 54.330 1.00 55.82 A ATOM 605 C MSE A 100 55.366 64.446 52.371 1.00 36.07 A ATOM 606 O MSE A 100 56.517 64.561 52.789 1.00 34.98 A ATOM 607 N LEU A 101 54.681 63.316 52.436 1.00 32.38 A ATOM 608 CA LEU A 101 55.238 62.126 53.031 1.00 31.39 A ATOM 609 CB LEU A 101 54.241 60.993 52.880 1.00 30.22 A ATOM 610 CG LEU A 101 54.616 59.676 53.538 1.00 29.99 A ATOM 611 CD1 LEU A 101 54.859 59.906 55.028 1.00 29.67 A ATOM 612 CD2 LEU A 101 53.501 58.674 53.287 1.00 26.62 A ATOM 613 C LEU A 101 56.571 61.745 52.394 1.00 31.59 A ATOM 614 O LEU A 101 57.523 61.341 53.077 1.00 32.03 A ATOM 615 N TYR A 102 56.624 61.872 51.076 1.00 30.32 A ATOM 616 CA TYR A 102 57.814 61.556 50.311 1.00 29.70 A ATOM 617 CB TYR A 102 57.550 61.840 48.838 1.00 29.09 A ATOM 618 CG TYR A 102 58.765 61.747 47.940 1.00 27.92 A ATOM 619 CD1 TYR A 102 59.402 60.530 47.709 1.00 27.22 A ATOM 620 CE1 TYR A 102 60.478 60.441 46.831 1.00 27.22 A ATOM 621 CD2 TYR A 102 59.243 62.873 47.274 1.00 26.92 A ATOM 622 CE2 TYR A 102 60.314 62.792 46.401 1.00 24.90 A ATOM 623 CZ TYR A 102 60.921 61.580 46.181 1.00 26.49 A ATOM 624 OH TYR A 102 61.959 61.497 45.299 1.00 26.37 A ATOM 625 C TYR A 102 58.970 62.409 50.796 1.00 30.50 A ATOM 626 O TYR A 102 60.057 61.905 51.125 1.00 30.28 A ATOM 627 N GLU A 103 58.731 63.715 50.839 1.00 31.34 A ATOM 628 CA GLU A 103 59.763 64.645 51.276 1.00 32.16 A ATOM 629 CB GLU A 103 59.314 66.088 50.966 1.00 32.79 A ATOM 630 CG GLU A 103 58.921 66.251 49.492 1.00 35.11 A ATOM 631 CD GLU A 103 58.538 67.673 49.065 1.00 37.94 A ATOM 632 OE1 GLU A 103 57.628 68.279 49.685 1.00 37.38 A ATOM 633 OE2 GLU A 103 59.138 68.175 48.084 1.00 37.07 A ATOM 634 C GLU A 103 60.128 64.438 52.760 1.00 30.98 A ATOM 635 O GLU A 103 61.292 64.600 53.136 1.00 30.87 A ATOM 636 N ILE A 104 59.159 64.038 53.588 1.00 29.27 A ATOM 637 CA ILE A 104 59.426 63.804 55.011 1.00 28.70 A ATOM 638 CB ILE A 104 58.113 63.589 55.813 1.00 28.55 A ATOM 639 CG2 ILE A 104 58.424 62.958 57.189 1.00 29.44 A ATOM 640 CG1 ILE A 104 57.396 64.942 55.975 1.00 26.70 A ATOM 641 CD1 ILE A 104 56.098 64.917 56.782 1.00 22.17 A ATOM 642 C ILE A 104 60.359 62.609 55.221 1.00 27.96 A ATOM 643 O ILE A 104 61.180 62.591 56.144 1.00 26.87 A ATOM 644 N ILE A 105 60.225 61.609 54.360 1.00 27.92 A ATOM 645 CA ILE A 105 61.082 60.439 54.435 1.00 26.71 A ATOM 646 CB ILE A 105 60.543 59.321 53.534 1.00 26.61 A ATOM 647 CG2 ILE A 105 61.590 58.215 53.388 1.00 25.95 A ATOM 648 CG1 ILE A 105 59.200 58.836 54.106 1.00 26.49 A ATOM 649 CD1 ILE A 105 58.546 57.701 53.349 1.00 26.37 A ATOM 650 C ILE A 105 62.500 60.825 54.017 1.00 26.46 A ATOM 651 O ILE A 105 63.484 60.401 54.639 1.00 26.10 A ATOM 652 N LEU A 106 62.603 61.648 52.975 1.00 25.01 A ATOM 653 CA LEU A 106 63.915 62.084 52.505 1.00 24.17 A ATOM 654 CB LEU A 106 63.802 62.917 51.230 1.00 23.30 A ATOM 655 CG LEU A 106 63.211 62.283 49.961 1.00 22.86 A ATOM 656 CD1 LEU A 106 63.415 63.252 48.829 1.00 19.46 A ATOM 657 CD2 LEU A 106 63.875 60.950 49.639 1.00 17.99 A ATOM 658 C LEU A 106 64.612 62.904 53.574 1.00 24.05 A ATOM 659 O LEU A 106 65.792 62.701 53.860 1.00 24.80 A ATOM 660 N ALA A 107 63.875 63.835 54.168 1.00 23.58 A ATOM 661 CA ALA A 107 64.430 64.676 55.218 1.00 23.64 A ATOM 662 CB ALA A 107 63.388 65.684 55.684 1.00 21.11 A ATOM 663 C ALA A 107 64.901 63.817 56.393 1.00 23.90 A ATOM 664 O ALA A 107 65.978 64.046 56.952 1.00 23.39 A ATOM 665 N ALA A 108 64.093 62.838 56.779 1.00 24.83 A ATOM 666 CA ALA A 108 64.479 61.970 57.879 1.00 27.43 A ATOM 667 CB ALA A 108 63.343 60.984 58.215 1.00 27.65 A ATOM 668 C ALA A 108 65.727 61.211 57.456 1.00 28.80 A ATOM 669 O ALA A 108 66.646 61.009 58.249 1.00 29.92 A ATOM 670 N ASN A 109 65.763 60.794 56.196 1.00 28.89 A ATOM 671 CA ASN A 109 66.920 60.062 55.719 1.00 29.68 A ATOM 672 CB ASN A 109 66.631 59.416 54.361 1.00 31.27 A ATOM 673 CG ASN A 109 67.744 58.480 53.915 1.00 31.80 A ATOM 674 OD1 ASN A 109 68.755 58.912 53.362 1.00 31.60 A ATOM 675 ND2 ASN A 109 67.568 57.186 54.178 1.00 32.93 A ATOM 676 C ASN A 109 68.153 60.956 55.628 1.00 30.29 A ATOM 677 O ASN A 109 69.248 60.524 55.959 1.00 30.81 A ATOM 678 N TYR A 110 67.992 62.197 55.177 1.00 31.42 A ATOM 679 CA TYR A 110 69.133 63.105 55.080 1.00 31.10 A ATOM 680 CB TYR A 110 68.756 64.363 54.312 1.00 29.98 A ATOM 681 CG TYR A 110 69.819 65.437 54.351 1.00 30.69 A ATOM 682 CD1 TYR A 110 71.057 65.237 53.736 1.00 29.71 A ATOM 683 CE1 TYR A 110 72.022 66.241 53.716 1.00 30.17 A ATOM 684 CD2 TYR A 110 69.571 66.674 54.965 1.00 31.52 A ATOM 685 CE2 TYR A 110 70.526 67.686 54.954 1.00 31.71 A ATOM 686 CZ TYR A 110 71.750 67.463 54.318 1.00 32.53 A ATOM 687 OH TYR A 110 72.680 68.481 54.226 1.00 33.63 A ATOM 688 C TYR A 110 69.620 63.515 56.463 1.00 31.73 A ATOM 689 O TYR A 110 70.818 63.603 56.694 1.00 32.81 A ATOM 690 N LEU A 111 68.682 63.770 57.371 1.00 30.92 A ATOM 691 CA LEU A 111 69.016 64.184 58.719 1.00 31.21 A ATOM 692 CB LEU A 111 67.870 64.994 59.317 1.00 28.89 A ATOM 693 CG LEU A 111 67.630 66.380 58.734 1.00 26.61 A ATOM 694 CD1 LEU A 111 66.251 66.831 59.141 1.00 24.78 A ATOM 695 CD2 LEU A 111 68.694 67.360 59.200 1.00 24.10 A ATOM 696 C LEU A 111 69.337 63.006 59.624 1.00 33.12 A ATOM 697 O LEU A 111 69.590 63.181 60.816 1.00 34.02 A ATOM 698 N ASN A 112 69.319 61.805 59.062 1.00 33.71 A ATOM 699 CA ASN A 112 69.620 60.588 59.820 1.00 34.83 A ATOM 700 CB ASN A 112 71.102 60.570 60.204 1.00 33.95 A ATOM 701 CG ASN A 112 71.644 59.164 60.365 1.00 33.26 A ATOM 702 OD1 ASN A 112 71.015 58.322 60.977 1.00 34.03 A ATOM 703 ND2 ASN A 112 72.820 58.913 59.813 1.00 34.72 A ATOM 704 C ASN A 112 68.764 60.460 61.091 1.00 35.67 A ATOM 705 O ASN A 112 69.272 60.582 62.209 1.00 37.75 A ATOM 706 N ILE A 113 67.472 60.203 60.906 1.00 35.48 A ATOM 707 CA ILE A 113 66.517 60.055 62.005 1.00 35.39 A ATOM 708 CB ILE A 113 65.531 61.253 62.034 1.00 35.97 A ATOM 709 CG2 ILE A 113 64.563 61.125 63.200 1.00 35.08 A ATOM 710 CG1 ILE A 113 66.307 62.567 62.154 1.00 36.19 A ATOM 711 CD1 ILE A 113 65.427 63.795 62.132 1.00 33.68 A ATOM 712 C ILE A 113 65.738 58.761 61.763 1.00 35.67 A ATOM 713 O ILE A 113 64.564 58.789 61.381 1.00 33.98 A ATOM 714 N LYS A 114 66.408 57.632 61.988 1.00 37.77 A ATOM 715 CA LYS A 114 65.827 56.299 61.775 1.00 39.09 A ATOM 716 CB LYS A 114 66.697 55.238 62.461 1.00 41.82 A ATOM 717 CG LYS A 114 67.835 54.703 61.601 1.00 45.96 A ATOM 718 CD LYS A 114 68.786 55.789 61.081 1.00 47.81 A ATOM 719 CE LYS A 114 69.952 55.145 60.306 1.00 49.70 A ATOM 720 NZ LYS A 114 69.498 54.249 59.161 1.00 51.87 A ATOM 721 C LYS A 114 64.372 56.128 62.216 1.00 37.68 A ATOM 722 O LYS A 114 63.521 55.697 61.438 1.00 38.17 A ATOM 723 N PRO A 115 64.076 56.435 63.484 1.00 36.13 A ATOM 724 CD PRO A 115 65.015 56.886 64.526 1.00 34.15 A ATOM 725 CA PRO A 115 62.715 56.314 64.011 1.00 34.44 A ATOM 726 CB PRO A 115 62.815 57.022 65.351 1.00 34.06 A ATOM 727 CG PRO A 115 64.220 56.680 65.777 1.00 35.33 A ATOM 728 C PRO A 115 61.694 56.968 63.076 1.00 33.56 A ATOM 729 O PRO A 115 60.658 56.384 62.763 1.00 33.50 A ATOM 730 N LEU A 116 62.001 58.179 62.622 1.00 31.71 A ATOM 731 CA LEU A 116 61.108 58.903 61.733 1.00 30.40 A ATOM 732 CB LEU A 116 61.583 60.347 61.567 1.00 29.42 A ATOM 733 CG LEU A 116 60.603 61.229 60.796 1.00 28.24 A ATOM 734 CD1 LEU A 116 59.268 61.223 61.507 1.00 28.18 A ATOM 735 CD2 LEU A 116 61.144 62.633 60.674 1.00 29.52 A ATOM 736 C LEU A 116 61.005 58.211 60.375 1.00 30.54 A ATOM 737 O LEU A 116 59.909 58.046 59.823 1.00 29.43 A ATOM 738 N LEU A 117 62.150 57.804 59.836 1.00 30.80 A ATOM 739 CA LEU A 117 62.193 57.097 58.555 1.00 30.78 A ATOM 740 CB LEU A 117 63.632 56.678 58.223 1.00 28.60 A ATOM 741 CG LEU A 117 63.843 55.833 56.966 1.00 27.90 A ATOM 742 CD1 LEU A 117 63.388 56.587 55.756 1.00 26.40 A ATOM 743 CD2 LEU A 117 65.304 55.467 56.830 1.00 29.33 A ATOM 744 C LEU A 117 61.311 55.856 58.624 1.00 32.57 A ATOM 745 O LEU A 117 60.403 55.675 57.800 1.00 33.66 A ATOM 746 N ASP A 118 61.588 55.002 59.608 1.00 32.30 A ATOM 747 CA ASP A 118 60.821 53.781 59.777 1.00 32.82 A ATOM 748 CB ASP A 118 61.241 53.035 61.046 1.00 34.51 A ATOM 749 CG ASP A 118 62.660 52.481 60.958 1.00 38.01 A ATOM 750 OD1 ASP A 118 63.075 52.088 59.841 1.00 37.92 A ATOM 751 OD2 ASP A 118 63.355 52.432 62.007 1.00 38.31 A ATOM 752 C ASP A 118 59.345 54.104 59.836 1.00 32.67 A ATOM 753 O ASP A 118 58.533 53.458 59.160 1.00 33.71 A ATOM 754 N ALA A 119 58.997 55.109 60.632 1.00 31.48 A ATOM 755 CA ALA A 119 57.600 55.512 60.774 1.00 32.03 A ATOM 756 CB ALA A 119 57.512 56.753 61.625 1.00 31.77 A ATOM 757 C ALA A 119 56.961 55.774 59.418 1.00 32.00 A ATOM 758 O ALA A 119 55.932 55.185 59.071 1.00 31.09 A ATOM 759 N GLY A 120 57.582 56.673 58.660 1.00 32.93 A ATOM 760 CA GLY A 120 57.081 57.007 57.341 1.00 33.63 A ATOM 761 C GLY A 120 57.019 55.773 56.469 1.00 33.78 A ATOM 762 O GLY A 120 56.045 55.571 55.748 1.00 33.76 A ATOM 763 N CYS A 121 58.056 54.944 56.522 1.00 34.09 A ATOM 764 CA CYS A 121 58.048 53.735 55.714 1.00 37.06 A ATOM 765 CB CYS A 121 59.370 52.985 55.852 1.00 37.59 A ATOM 766 SG CYS A 121 60.672 53.684 54.825 1.00 37.93 A ATOM 767 C CYS A 121 56.882 52.814 56.063 1.00 36.49 A ATOM 768 O CYS A 121 56.222 52.272 55.177 1.00 37.36 A ATOM 769 N LYS A 122 56.617 52.645 57.348 1.00 36.54 A ATOM 770 CA LYS A 122 55.525 51.786 57.766 1.00 37.44 A ATOM 771 CB LYS A 122 55.445 51.751 59.288 1.00 38.22 A ATOM 772 CG LYS A 122 56.652 51.150 59.950 1.00 38.67 A ATOM 773 CD LYS A 122 56.424 51.081 61.441 1.00 42.04 A ATOM 774 CE LYS A 122 57.663 50.592 62.185 1.00 42.25 A ATOM 775 NZ LYS A 122 57.394 50.419 63.636 1.00 41.74 A ATOM 776 C LYS A 122 54.197 52.276 57.208 1.00 36.82 A ATOM 777 O LYS A 122 53.340 51.479 56.812 1.00 36.50 A ATOM 778 N VAL A 123 54.035 53.595 57.187 1.00 36.30 A ATOM 779 CA VAL A 123 52.810 54.208 56.699 1.00 35.72 A ATOM 780 CB VAL A 123 52.832 55.718 56.967 1.00 36.26 A ATOM 781 CG1 VAL A 123 51.483 56.319 56.621 1.00 36.90 A ATOM 782 CG2 VAL A 123 53.170 55.966 58.429 1.00 35.63 A ATOM 783 C VAL A 123 52.576 53.929 55.208 1.00 35.46 A ATOM 784 O VAL A 123 51.448 53.633 54.793 1.00 33.96 A ATOM 785 N VAL A 124 53.639 54.007 54.406 1.00 35.31 A ATOM 786 CA VAL A 124 53.510 53.737 52.970 1.00 34.89 A ATOM 787 CB VAL A 124 54.815 54.026 52.177 1.00 34.43 A ATOM 788 CG1 VAL A 124 54.564 53.832 50.682 1.00 32.55 A ATOM 789 CG2 VAL A 124 55.294 55.442 52.449 1.00 34.56 A ATOM 790 C VAL A 124 53.135 52.273 52.767 1.00 34.07 A ATOM 791 O VAL A 124 52.317 51.947 51.898 1.00 34.52 A ATOM 792 N ALA A 125 53.734 51.401 53.575 1.00 32.52 A ATOM 793 CA ALA A 125 53.452 49.974 53.500 1.00 33.46 A ATOM 794 CB ALA A 125 54.294 49.221 54.496 1.00 31.49 A ATOM 795 C ALA A 125 51.975 49.757 53.805 1.00 35.59 A ATOM 796 O ALA A 125 51.283 48.987 53.127 1.00 35.62 A ATOM 797 N GLU A 126 51.495 50.462 54.823 1.00 37.35 A ATOM 798 CA GLU A 126 50.107 50.357 55.213 1.00 37.88 A ATOM 799 CB GLU A 126 49.864 51.130 56.494 1.00 39.94 A ATOM 800 CG GLU A 126 50.589 50.522 57.658 1.00 44.44 A ATOM 801 CD GLU A 126 49.884 50.789 58.974 1.00 47.25 A ATOM 802 OE1 GLU A 126 49.926 51.949 59.454 1.00 46.76 A ATOM 803 OE2 GLU A 126 49.271 49.832 59.516 1.00 49.61 A ATOM 804 C GLU A 126 49.149 50.812 54.142 1.00 37.12 A ATOM 805 O GLU A 126 47.974 50.472 54.189 1.00 36.85 A ATOM 806 N MSE A 127 49.648 51.573 53.176 1.00 37.83 A ATOM 807 CA MSE A 127 48.814 52.035 52.085 1.00 38.50 A ATOM 808 CB MSE A 127 49.473 53.225 51.396 1.00 39.64 A ATOM 809 CG MSE A 127 49.682 54.471 52.264 1.00 40.86 A ATOM 810 SE MSE A 127 50.428 55.994 51.160 1.00 44.01 A ATOM 811 CE MSE A 127 48.774 56.477 50.261 1.00 43.47 A ATOM 812 C MSE A 127 48.621 50.885 51.092 1.00 38.76 A ATOM 813 O MSE A 127 47.586 50.792 50.443 1.00 38.95 A ATOM 814 N ILE A 128 49.607 49.997 51.003 1.00 39.74 A ATOM 815 CA ILE A 128 49.552 48.849 50.090 1.00 40.70 A ATOM 816 CB ILE A 128 50.989 48.359 49.755 1.00 39.21 A ATOM 817 CG2 ILE A 128 50.935 47.158 48.828 1.00 39.17 A ATOM 818 CG1 ILE A 128 51.797 49.518 49.163 1.00 37.59 A ATOM 819 CD1 ILE A 128 53.148 49.159 48.595 1.00 35.03 A ATOM 820 C ILE A 128 48.777 47.698 50.736 1.00 42.24 A ATOM 821 O ILE A 128 47.886 47.098 50.132 1.00 40.92 A ATOM 822 N ARG A 129 49.147 47.412 51.980 1.00 46.16 A ATOM 823 CA ARG A 129 48.556 46.350 52.792 1.00 49.18 A ATOM 824 CB ARG A 129 48.696 46.701 54.268 1.00 50.29 A ATOM 825 CG ARG A 129 48.224 45.614 55.205 1.00 53.92 A ATOM 826 CD ARG A 129 48.566 45.978 56.643 1.00 58.68 A ATOM 827 NE ARG A 129 49.936 46.490 56.743 1.00 62.87 A ATOM 828 CZ ARG A 129 50.553 46.798 57.881 1.00 64.32 A ATOM 829 NH1 ARG A 129 49.927 46.647 59.045 1.00 64.82 A ATOM 830 NH2 ARG A 129 51.799 47.258 57.850 1.00 64.62 A ATOM 831 C ARG A 129 47.094 46.044 52.498 1.00 49.27 A ATOM 832 O ARG A 129 46.230 46.920 52.589 1.00 49.24 A ATOM 833 N GLY A 130 46.839 44.785 52.158 1.00 48.73 A ATOM 834 CA GLY A 130 45.492 44.354 51.873 1.00 49.33 A ATOM 835 C GLY A 130 44.843 44.937 50.632 1.00 50.07 A ATOM 836 O GLY A 130 43.619 44.856 50.486 1.00 49.22 A ATOM 837 N ARG A 131 45.630 45.523 49.735 1.00 49.98 A ATOM 838 CA ARG A 131 45.048 46.086 48.524 1.00 50.73 A ATOM 839 CB ARG A 131 45.402 47.573 48.410 1.00 51.87 A ATOM 840 CG ARG A 131 44.801 48.429 49.545 1.00 54.75 A ATOM 841 CD ARG A 131 45.035 49.929 49.340 1.00 57.52 A ATOM 842 NE ARG A 131 44.412 50.438 48.116 1.00 60.43 A ATOM 843 CZ ARG A 131 43.098 50.531 47.910 1.00 61.10 A ATOM 844 NH1 ARG A 131 42.248 50.147 48.855 1.00 60.79 A ATOM 845 NH2 ARG A 131 42.634 51.009 46.755 1.00 61.77 A ATOM 846 C ARG A 131 45.447 45.325 47.261 1.00 50.69 A ATOM 847 O ARG A 131 46.432 44.592 47.249 1.00 51.15 A ATOM 848 N SER A 132 44.670 45.494 46.199 1.00 50.35 A ATOM 849 CA SER A 132 44.941 44.798 44.950 1.00 50.32 A ATOM 850 CB SER A 132 43.630 44.489 44.224 1.00 49.61 A ATOM 851 OG SER A 132 43.082 45.662 43.648 1.00 48.59 A ATOM 852 G SER A 132 45.837 45.608 44.023 1.00 50.87 A ATOM 853 O SER A 132 46.056 46.808 44.235 1.00 50.23 A ATOM 854 N PRO A 133 46.359 44.957 42.970 1.00 50.57 A ATOM 855 CD PRO A 133 46.253 43.520 42.659 1.00 49.65 A ATOM 856 CA PRO A 133 47.230 45.628 42.006 1.00 50.93 A ATOM 857 CB PRO A 133 47.392 44.581 40.914 1.00 50.37 A ATOM 858 CG PRO A 133 47.405 43.315 41.698 1.00 50.36 A ATOM 859 C PRO A 133 46.616 46.915 41.483 1.00 51.56 A ATOM 860 O PRO A 133 47.263 47.964 41.480 1.00 52.20 A ATOM 861 N GLU A 134 45.364 46.839 41.044 1.00 51.94 A ATOM 862 CA GLU A 134 44.693 48.021 40.516 1.00 52.22 A ATOM 863 CB GLU A 134 43.395 47.637 39.811 1.00 54.08 A ATOM 864 CG GLU A 134 43.436 47.886 38.314 1.00 58.97 A ATOM 865 CD GLU A 134 43.821 49.320 37.974 1.00 62.39 A ATOM 866 OE1 GLU A 134 43.122 50.254 38.436 1.00 63.15 A ATOM 867 OE2 GLU A 134 44.823 49.513 37.243 1.00 64.67 A ATOM 868 C GLU A 134 44.406 49.035 41.610 1.00 50.15 A ATOM 869 O GLU A 134 44.400 50.244 41.355 1.00 49.58 A ATOM 870 N GLU A 135 44.177 48.539 42.823 1.00 47.26 A ATOM 871 CA GLU A 135 43.904 49.412 43.948 1.00 45.19 A ATOM 872 CB GLU A 135 43.390 48.613 45.142 1.00 44.69 A ATOM 873 CG GLU A 135 41.973 48.135 44.948 1.00 47.13 A ATOM 874 CD GLU A 135 41.333 47.585 46.207 1.00 49.00 A ATOM 875 OE1 GLU A 135 41.857 46.590 46.766 1.00 49.49 A ATOM 876 OE2 GLU A 135 40.295 48.153 46.633 1.00 50.00 A ATOM 877 C GLU A 135 45.160 50.162 44.328 1.00 43.66 A ATOM 878 O GLU A 135 45.113 51.349 44.650 1.00 42.57 A ATOM 879 N ILE A 136 46.288 49.467 44.269 1.00 41.78 A ATOM 880 CA ILE A 136 47.558 50.077 44.622 1.00 41.23 A ATOM 881 CB ILE A 136 48.646 49.014 44.782 1.00 39.22 A ATOM 882 CG2 ILE A 136 49.957 49.675 45.197 1.00 37.75 A ATOM 883 CG1 ILE A 136 48.180 47.970 45.801 1.00 37.01 A ATOM 884 CD1 ILE A 136 49.154 46.847 46.033 1.00 34.37 A ATOM 885 C ILE A 136 47.993 51.065 43.558 1.00 42.50 A ATOM 886 O ILE A 136 48.490 52.162 43.856 1.00 42.93 A ATOM 887 N ARG A 137 47.787 50.651 42.314 1.00 42.34 A ATOM 888 CA ARG A 137 48.144 51.439 41.151 1.00 41.82 A ATOM 889 CB ARG A 137 47.844 50.636 39.884 1.00 42.65 A ATOM 890 CG ARG A 137 48.949 50.635 38.849 1.00 43.90 A ATOM 891 CD ARG A 137 48.594 49.715 37.679 1.00 45.63 A ATOM 892 NE ARG A 137 48.503 48.315 38.092 1.00 47.76 A ATOM 893 CZ ARG A 137 47.567 47.477 37.664 1.00 48.21 A ATOM 894 NH1 ARG A 137 46.644 47.901 36.810 1.00 49.10 A ATOM 895 NH2 ARG A 137 47.546 46.226 38.099 1.00 48.10 A ATOM 896 C ARG A 137 47.348 52.736 41.156 1.00 40.67 A ATOM 897 O ARG A 137 47.821 53.773 40.685 1.00 39.93 A ATOM 898 N ARG A 138 46.134 52.677 41.694 1.00 40.67 A ATOM 899 CA ARG A 138 45.276 53.864 41.756 1.00 40.88 A ATOM 900 CB ARG A 138 43.807 53.456 41.932 1.00 39.95 A ATOM 901 CG ARG A 138 43.140 52.934 40.660 0.00 41.86 A ATOM 902 CD ARG A 138 43.070 53.989 39.550 0.00 42.76 A ATOM 903 NE ARG A 138 44.301 54.072 38.764 0.00 43.72 A ATOM 904 CZ ARG A 138 44.443 54.802 37.659 0.00 44.10 A ATOM 905 NH1 ARG A 138 43.430 55.523 37.196 0.00 44.35 A ATOM 906 NH2 ARG A 138 45.602 54.812 37.015 0.00 44.35 A ATOM 907 C ARG A 138 45.706 54.791 42.895 1.00 39.80 A ATOM 908 O ARG A 138 45.705 56.016 42.762 1.00 39.09 A ATOM 909 N THR A 139 46.083 54.177 44.008 1.00 39.87 A ATOM 910 CA THR A 139 46.544 54.877 45.193 1.00 39.93 A ATOM 911 CB THR A 139 47.058 53.872 46.234 1.00 40.30 A ATOM 912 OG1 THR A 139 45.971 53.054 46.689 1.00 40.58 A ATOM 913 CG2 THR A 139 47.684 54.602 47.420 1.00 41.79 A ATOM 914 C THR A 139 47.674 55.849 44.881 1.00 41.13 A ATOM 915 O THR A 139 47.752 56.941 45.455 1.00 42.14 A ATOM 916 N PHE A 140 48.559 55.443 43.978 1.00 41.08 A ATOM 917 CA PHE A 140 49.705 56.267 43.607 1.00 39.57 A ATOM 918 CB PHE A 140 50.986 55.449 43.755 1.00 38.91 A ATOM 919 CG PHE A 140 51.220 54.943 45.145 1.00 38.38 A ATOM 920 CD1 PHE A 140 51.519 55.824 46.174 1.00 38.13 A ATOM 921 CD2 PHE A 140 51.122 53.588 45.432 1.00 37.94 A ATOM 922 GE1 PHE A 140 51.722 55.364 47.464 1.00 38.18 A ATOM 923 GE2 PHE A 140 51.323 53.118 46.721 1.00 37.42 A ATOM 924 CZ PHE A 140 51.622 54.008 47.739 1.00 38.51 A ATOM 925 C PHE A 140 49.600 56.779 42.185 1.00 39.01 A ATOM 926 O PHE A 140 50.512 57.434 41.685 1.00 39.06 A ATOM 927 N ASN A 141 48.485 56.483 41.537 1.00 38.54 A ATOM 928 CA ASN A 141 48.294 56.894 40.162 1.00 38.58 A ATOM 929 CB ASN A 141 48.220 58.407 40.049 1.00 39.46 A ATOM 930 CG ASN A 141 47.787 58.847 38.669 1.00 41.82 A ATOM 931 OD1 ASN A 141 46.655 58.592 38.257 1.00 44.53 A ATOM 932 ND2 ASN A 141 48.687 59.495 37.938 1.00 42.34 A ATOM 933 C ASN A 141 49.439 56.378 39.296 1.00 38.74 A ATOM 934 O ASN A 141 50.031 57.122 38.503 1.00 38.59 A ATOM 935 N ILE A 142 49.738 55.093 39.459 1.00 38.05 A ATOM 936 CA ILE A 142 50.800 54.429 38.715 1.00 37.68 A ATOM 937 CB ILE A 142 51.425 53.321 39.561 1.00 36.00 A ATOM 938 CG2 ILE A 142 52.451 52.563 38.755 1.00 34.95 A ATOM 939 CG1 ILE A 142 52.021 53.921 40.829 1.00 35.82 A ATOM 940 CD1 ILE A 142 52.449 52.875 41.837 1.00 36.82 A ATOM 941 C ILE A 142 50.239 53.819 37.440 1.00 38.81 A ATOM 942 O ILE A 142 49.121 53.321 37.441 1.00 39.45 A ATOM 943 N VAL A 143 51.022 53.855 36.361 1.00 40.31 A ATOM 944 CA VAL A 143 50.620 53.310 35.053 1.00 40.27 A ATOM 945 CB VAL A 143 51.373 54.017 33.905 1.00 42.11 A ATOM 946 CG1 VAL A 143 51.035 53.348 32.567 1.00 42.72 A ATOM 947 CG2 VAL A 143 51.016 55.493 33.877 1.00 41.43 A ATOM 948 C VAL A 143 50.868 51.808 34.881 1.00 39.19 A ATOM 949 O VAL A 143 51.955 51.309 35.172 1.00 38.15 A ATOM 950 N ASN A 144 49.869 51.107 34.359 1.00 38.94 A ATOM 951 CA ASN A 144 49.968 49.670 34.137 1.00 39.16 A ATOM 952 CB ASN A 144 48.575 49.048 34.256 1.00 39.51 A ATOM 953 CG ASN A 144 48.570 47.573 33.959 1.00 40.78 A ATOM 954 OD1 ASN A 144 49.586 46.903 34.090 1.00 44.00 A ATOM 955 ND2 ASN A 144 47.421 47.052 33.574 1.00 41.05 A ATOM 956 C ASN A 144 50.582 49.341 32.775 1.00 38.55 A ATOM 957 O ASN A 144 49.876 48.975 31.839 1.00 37.91 A ATOM 958 N ASP A 145 51.902 49.448 32.685 1.00 38.25 A ATOM 959 CA ASP A 145 52.624 49.190 31.440 1.00 39.85 A ATOM 960 CB ASP A 145 53.996 49.862 31.498 1.00 39.46 A ATOM 961 CG ASP A 145 54.766 49.490 32.750 1.00 39.69 A ATOM 962 OD1 ASP A 145 54.213 48.735 33.587 1.00 39.21 A ATOM 963 OD2 ASP A 145 55.918 49.947 32.895 1.00 38.21 A ATOM 964 C ASP A 145 52.798 47.712 31.092 1.00 40.13 A ATOM 965 O ASP A 145 53.702 47.343 30.337 1.00 39.56 A ATOM 966 N PHE A 146 51.938 46.870 31.652 1.00 40.47 A ATOM 967 CA PHE A 146 51.978 45.440 31.377 1.00 40.10 A ATOM 968 CB PHE A 146 51.371 44.644 32.541 1.00 39.31 A ATOM 969 CG PHE A 146 52.301 44.453 33.699 1.00 40.02 A ATOM 970 CD1 PHE A 146 53.534 43.850 33.520 1.00 39.21 A ATOM 971 CD2 PHE A 146 51.952 44.889 34.971 1.00 39.97 A ATOM 972 CE1 PHE A 146 54.407 43.690 34.591 1.00 39.41 A ATOM 973 CE2 PHE A 146 52.827 44.731 36.051 1.00 38.93 A ATOM 974 CZ PHE A 146 54.053 44.131 35.858 1.00 38.17 A ATOM 975 C PHE A 146 51.167 45.171 30.113 1.00 40.82 A ATOM 976 O PHE A 146 50.013 45.603 29.999 1.00 41.89 A ATOM 977 N THR A 147 51.773 44.476 29.154 1.00 40.38 A ATOM 978 CA THR A 147 51.073 44.137 27.922 1.00 38.81 A ATOM 979 CB THR A 147 51.999 43.509 26.877 1.00 38.98 A ATOM 980 OG1 THR A 147 52.651 42.373 27.456 1.00 39.24 A ATOM 981 CG2 THR A 147 53.030 44.498 26.395 1.00 36.50 A ATOM 982 C THR A 147 50.062 43.070 28.286 1.00 38.78 A ATOM 983 O THR A 147 50.233 42.343 29.268 1.00 37.08 A ATOM 984 N PRO A 148 49.003 42.943 27.485 1.00 39.53 A ATOM 985 CD PRO A 148 48.718 43.722 26.266 1.00 39.08 A ATOM 986 CA PRO A 148 47.958 41.947 27.732 1.00 40.59 A ATOM 987 CB PRO A 148 47.166 41.970 26.428 1.00 39.52 A ATOM 988 CG PRO A 148 47.260 43.419 26.034 1.00 39.40 A ATOM 989 C PRO A 148 48.505 40.545 28.078 1.00 42.69 A ATOM 990 O PRO A 148 48.007 39.876 28.984 1.00 43.05 A ATOM 991 N GLU A 149 49.546 40.123 27.370 1.00 45.32 A ATOM 992 CA GLU A 149 50.155 38.814 27.572 1.00 46.47 A ATOM 993 CB GLU A 149 51.059 38.496 26.395 1.00 44.18 A ATOM 994 CG GLU A 149 51.681 37.137 26.430 1.00 43.56 A ATOM 995 CD GLU A 149 52.660 36.955 25.311 1.00 43.86 A ATOM 996 OE1 GLU A 149 53.660 37.699 25.279 1.00 43.12 A ATOM 997 OE2 GLU A 149 52.430 36.075 24.458 1.00 44.44 A ATOM 998 C GLU A 149 50.974 38.773 28.845 1.00 48.79 A ATOM 999 O GLU A 149 50.852 37.856 29.660 1.00 49.11 A ATOM 1000 N GLU A 150 51.826 39.773 29.006 1.00 52.88 A ATOM 1001 CA GLU A 150 52.676 39.855 30.180 1.00 56.79 A ATOM 1002 CB GLU A 150 53.548 41.105 30.090 1.00 56.56 A ATOM 1003 CG GLU A 150 54.707 41.109 31.045 1.00 57.96 A ATOM 1004 CD GLU A 150 55.774 40.103 30.660 1.00 59.33 A ATOM 1005 OE1 GLU A 150 55.489 38.887 30.639 1.00 60.34 A ATOM 1006 OE2 GLU A 150 56.907 40.533 30.372 1.00 60.87 A ATOM 1007 C GLU A 150 51.804 39.913 31.433 1.00 59.23 A ATOM 1008 O GLU A 150 52.187 39.417 32.488 1.00 59.36 A ATOM 1009 N GLU A 151 50.627 40.519 31.305 1.00 62.33 A ATOM 1010 CA GLU A 151 49.701 40.651 32.424 1.00 64.96 A ATOM 1011 CB GLU A 151 48.477 41.452 31.982 1.00 65.44 A ATOM 1012 CG GLU A 151 48.102 42.579 32.923 1.00 66.38 A ATOM 1013 CD GLU A 151 47.141 43.563 32.287 1.00 67.52 A ATOM 1014 OE1 GLU A 151 47.510 44.187 31.269 1.00 67.49 A ATOM 1015 OE2 GLU A 151 46.014 43.713 32.803 1.00 68.18 A ATOM 1016 C GLU A 151 49.270 39.286 32.954 1.00 66.62 A ATOM 1017 O GLU A 151 49.543 38.943 34.104 1.00 66.87 A ATOM 1018 N ALA A 152 48.602 38.512 32.106 1.00 68.29 A ATOM 1019 CA ALA A 152 48.137 37.181 32.474 1.00 70.15 A ATOM 1020 CB ALA A 152 47.511 36.503 31.268 1.00 70.09 A ATOM 1021 C ALA A 152 49.280 36.327 33.014 1.00 71.79 A ATOM 1022 O ALA A 152 49.085 35.503 33.903 1.00 71.18 A ATOM 1023 N ALA A 153 50.477 36.526 32.475 1.00 74.38 A ATOM 1024 CA ALA A 153 51.632 35.761 32.917 1.00 76.96 A ATOM 1025 CB ALA A 153 52.834 36.056 32.020 1.00 76.52 A ATOM 1026 C ALA A 153 51.969 36.069 34.376 1.00 79.23 A ATOM 1027 O ALA A 153 53.040 35.700 34.863 1.00 80.18 A ATOM 1028 N ILE A 154 51.061 36.759 35.067 1.00 80.86 A ATOM 1029 CA ILE A 154 51.257 37.103 36.479 1.00 82.60 A ATOM 1030 CB ILE A 154 51.680 38.592 36.656 1.00 81.99 A ATOM 1031 CG2 ILE A 154 51.889 38.898 38.134 0.00 82.34 A ATOM 1032 CG1 ILE A 154 52.986 38.866 35.905 1.00 81.41 A ATOM 1033 CD1 ILE A 154 53.347 40.336 35.822 0.00 81.80 A ATOM 1034 C ILE A 154 49.976 36.834 37.285 1.00 83.80 A ATOM 1035 O ILE A 154 49.036 37.633 37.272 1.00 83.56 A ATOM 1036 N ARG A 155 49.956 35.697 37.982 1.00 85.60 A ATOM 1037 CA ARG A 155 48.807 35.284 38.783 1.00 86.76 A ATOM 1038 CB ARG A 155 48.632 36.208 39.992 0.00 87.40 A ATOM 1039 CG ARG A 155 49.431 35.788 41.222 0.00 88.39 A ATOM 1040 CD ARG A 155 50.925 35.725 40.946 0.00 89.22 A ATOM 1041 NE ARG A 155 51.668 35.196 42.087 0.00 89.99 A ATOM 1042 CZ ARG A 155 51.561 33.949 42.535 0.00 90.38 A ATOM 1043 NH1 ARG A 155 50.740 33.095 41.937 0.00 90.63 A ATOM 1044 NH2 ARG A 155 52.272 33.555 43.584 0.00 90.63 A ATOM 1045 C ARG A 155 47.543 35.286 37.933 1.00 87.04 A ATOM 1046 O ARG A 155 46.710 36.199 38.125 1.00 87.33 A ATOM 1047 OXT ARG A 155 47.413 34.380 37.075 1.00 86.76 A ATOM 1048 CB LED B 270 49.350 65.486 42.241 1.00 56.04 B ATOM 1049 CG LED B 270 48.859 64.640 41.059 1.00 56.55 B ATOM 1050 CD1 LED B 270 47.337 64.629 41.020 1.00 55.59 B ATOM 1051 CD2 LEU B 270 49.424 65.209 39.762 1.00 56.75 B ATOM 1052 C LED B 270 49.537 63.882 44.208 1.00 54.79 B ATOM 1053 O LEU B 270 50.136 63.918 45.287 1.00 55.23 B ATOM 1054 N LED B 270 49.056 66.304 44.560 1.00 56.05 B ATOM 1055 CA LED B 270 48.835 65.142 43.652 1.00 55.53 B ATOM 1056 N LYS B 271 49.463 62.779 43.462 1.00 52.96 B ATOM 1057 CA LYS B 271 50.053 61.495 43.865 1.00 49.38 B ATOM 1058 CB LYS B 271 49.292 60.338 43.210 1.00 48.76 B ATOM 1059 CG LYS B 271 47.793 60.523 43.065 1.00 48.20 B ATOM 1060 CD LYS B 271 47.049 59.967 44.264 1.00 48.26 B ATOM 1061 CE LYS B 271 45.545 59.892 44.014 1.00 46.84 B ATOM 1062 NZ LYS B 271 45.188 59.152 42.766 1.00 47.61 B ATOM 1063 C LYS B 271 51.521 61.364 43.462 1.00 47.55 B ATOM 1064 O LYS B 271 52.069 62.218 42.764 1.00 47.27 B ATOM 1065 N ARG B 272 52.138 60.263 43.883 1.00 45.44 B ATOM 1066 CA ARG B 272 53.529 59.981 43.558 1.00 42.97 B ATOM 1067 CB ARG B 272 54.444 60.845 44.404 1.00 42.52 B ATOM 1068 CG ARG B 272 55.897 60.542 44.181 1.00 44.05 B ATOM 1069 CD ARG B 272 56.741 61.677 44.691 1.00 45.19 B ATOM 1070 NE ARG B 272 57.927 61.836 43.866 1.00 46.68 B ATOM 1071 CZ ARG B 272 58.416 63.009 43.491 1.00 47.36 B ATOM 1072 NH1 ARG B 272 57.816 64.130 43.868 1.00 46.52 B ATOM 1073 NH2 ARG B 272 59.505 63.056 42.737 1.00 48.34 B ATOM 1074 C ARG B 272 53.911 58.517 43.753 1.00 41.43 B ATOM 1075 O ARG B 272 53.678 57.944 44.816 1.00 41.22 B ATOM 1076 N ASP B 273 54.495 57.911 42.724 1.00 39.99 B ATOM 1077 CA ASP B 273 54.914 56.517 42.821 1.00 37.49 B ATOM 1078 CB ASP B 273 55.435 56.006 41.487 1.00 38.41 B ATOM 1079 CG ASP B 273 55.631 54.508 41.482 1.00 40.70 B ATOM 1080 OD1 ASP B 273 56.269 53.969 42.423 1.00 39.39 B ATOM 1081 OD2 ASP B 273 55.143 53.874 40.525 1.00 43.85 B ATOM 1082 C ASP B 273 56.040 56.474 43.829 1.00 35.40 B ATOM 1083 O ASP B 273 57.218 56.453 43.463 1.00 33.99 B ATOM 1084 N LEU B 274 55.671 56.460 45.101 1.00 33.28 B ATOM 1085 CA LEU B 274 56.646 56.450 46.170 1.00 32.55 B ATOM 1086 CB LEU B 274 55.937 56.322 47.514 1.00 32.85 B ATOM 1087 CG LEU B 274 55.728 57.659 48.229 1.00 34.16 B ATOM 1088 CD1 LEU B 274 54.930 58.598 47.361 1.00 33.65 B ATOM 1089 CD2 LEU B 274 55.035 57.421 49.561 1.00 35.07 B ATOM 1090 C LEU B 274 57.723 55.391 46.066 1.00 31.70 B ATOM 1091 O LEU B 274 58.903 55.687 46.250 1.00 31.68 B ATOM 1092 N ILE B 275 57.338 54.160 45.756 1.00 31.28 B ATOM 1093 CA ILE B 275 58.338 53.115 45.687 1.00 30.61 B ATOM 1094 CB ILE B 275 57.703 51.700 45.636 1.00 31.77 B ATOM 1095 CG2 ILE B 275 56.364 51.696 46.322 1.00 29.79 B ATOM 1096 CG1 ILE B 275 57.579 51.245 44.196 1.00 34.36 B ATOM 1097 CD1 ILE B 275 58.058 49.838 44.000 1.00 34.82 B ATOM 1098 C ILE B 275 59.325 53.301 44.535 1.00 29.10 B ATOM 1099 O ILE B 275 60.495 52.944 44.675 1.00 28.41 B ATOM 1100 N THR B 276 58.893 53.846 43.398 1.00 28.07 B ATOM 1101 CA THR B 276 59.875 54.056 42.336 1.00 29.79 B ATOM 1102 CB THR B 276 59.259 54.160 40.906 1.00 29.82 B ATOM 1103 OG1 THR B 276 58.327 55.236 40.859 1.00 33.40 B ATOM 1104 CG2 THR B 276 58.569 52.869 40.507 1.00 31.42 B ATOM 1105 C THR B 276 60.718 55.314 42.580 1.00 28.87 B ATOM 1106 O THR B 276 61.885 55.341 42.222 1.00 29.74 B ATOM 1107 N SER B 277 60.145 56.333 43.211 1.00 27.47 B ATOM 1108 CA SER B 277 60.867 57.567 43.454 1.00 27.08 B ATOM 1109 CB SER B 277 59.877 58.706 43.664 1.00 28.54 B ATOM 1110 OG SER B 277 59.027 58.861 42.533 1.00 29.07 B ATOM 1111 C SER B 277 61.843 57.511 44.622 1.00 28.04 B ATOM 1112 O SER B 277 62.850 58.200 44.607 1.00 29.44 B ATOM 1113 N LEU B 278 61.546 56.717 45.644 1.00 28.55 B ATOM 1114 CA LEU B 278 62.443 56.606 46.786 1.00 28.04 B ATOM 1115 CB LEU B 278 61.777 55.854 47.921 1.00 27.87 B ATOM 1116 CG LEU B 278 61.098 56.650 49.043 1.00 29.93 B ATOM 1117 CD1 LEU B 278 62.130 57.593 49.658 1.00 30.19 B ATOM 1118 CD2 LEU B 278 59.898 57.407 48.526 1.00 28.70 B ATOM 1119 C LEU B 278 63.697 55.857 46.401 1.00 29.78 B ATOM 1120 O LEU B 278 63.728 55.140 45.398 1.00 30.41 B ATOM 1121 N PRO B 279 64.771 56.039 47.171 1.00 30.02 B ATOM 1122 CD PRO B 279 65.103 57.050 48.187 1.00 29.94 B ATOM 1123 CA PRO B 279 65.948 55.281 46.764 1.00 30.32 B ATOM 1124 CB PRO B 279 67.068 55.907 47.584 1.00 29.20 B ATOM 1125 CG PRO B 279 66.371 56.499 48.763 1.00 31.41 B ATOM 1126 C PRO B 279 65.690 53.813 47.094 1.00 32.64 B ATOM 1127 O PRO B 279 64.946 53.494 48.026 1.00 32.21 B ATOM 1128 N PHE B 280 66.291 52.927 46.308 1.00 34.93 B ATOM 1129 CA PHE B 280 66.122 51.495 46.476 1.00 35.83 B ATOM 1130 CB PHE B 280 67.177 50.745 45.671 1.00 35.18 B ATOM 1131 CG PHE B 280 67.040 49.266 45.752 1.00 35.73 B ATOM 1132 CD1 PHE B 280 65.871 48.644 45.307 1.00 35.82 B ATOM 1133 CD2 PHE B 280 68.050 48.493 46.319 1.00 34.88 B ATOM 1134 CE1 PHE B 280 65.703 47.266 45.430 1.00 37.94 B ATOM 1135 CE2 PHE B 280 67.897 47.111 46.452 1.00 36.63 B ATOM 1136 CZ PHE B 280 66.717 46.489 46.006 1.00 36.74 B ATOM 1137 C PHE B 280 66.172 51.017 47.917 1.00 37.41 B ATOM 1138 O PHE B 280 65.263 50.331 48.371 1.00 39.64 B ATOM 1139 N GLU B 281 67.235 51.366 48.634 1.00 38.02 B ATOM 1140 CA GLU B 281 67.391 50.934 50.017 1.00 38.96 B ATOM 1141 CB GLU B 281 68.622 51.584 50.659 1.00 42.67 B ATOM 1142 CG GLU B 281 69.932 51.424 49.875 1.00 49.17 B ATOM 1143 CD GLU B 281 70.188 49.992 49.394 1.00 51.93 B ATOM 1144 OE1 GLU B 281 69.840 49.030 50.127 1.00 51.55 B ATOM 1145 OE2 GLU B 281 70.747 49.845 48.276 1.00 53.97 B ATOM 1146 C GLU B 281 66.169 51.251 50.859 1.00 38.70 B ATOM 1147 O GLU B 281 65.863 50.516 51.796 1.00 40.56 B ATOM 1148 N ILE B 282 65.472 52.338 50.531 1.00 36.39 B ATOM 1149 CA ILE B 282 64.289 52.728 51.291 1.00 33.47 B ATOM 1150 CB ILE B 282 64.019 54.250 51.194 1.00 33.48 B ATOM 1151 CG2 ILE B 282 62.633 54.581 51.721 1.00 31.07 B ATOM 1152 CG1 ILE B 282 65.091 55.007 51.974 1.00 33.33 B ATOM 1153 CD1 ILE B 282 64.849 56.494 52.090 1.00 35.69 B ATOM 1154 C ILE B 282 63.030 51.984 50.891 1.00 32.60 B ATOM 1155 O ILE B 282 62.238 51.614 51.748 1.00 33.74 B ATOM 1156 N SER B 283 62.833 51.753 49.602 1.00 32.28 B ATOM 1157 CA SER B 283 61.632 51.052 49.180 1.00 31.76 B ATOM 1158 CB SER B 283 61.531 51.043 47.665 1.00 30.24 B ATOM 1159 OG SER B 283 60.948 52.260 47.227 1.00 30.65 B ATOM 1160 C SER B 283 61.554 49.642 49.732 1.00 32.64 B ATOM 1161 O SER B 283 60.460 49.145 50.033 1.00 31.74 B ATOM 1162 N LEU B 284 62.715 49.011 49.891 1.00 34.08 B ATOM 1163 CA LEU B 284 62.761 47.661 50.433 1.00 36.79 B ATOM 1164 CB LEU B 284 64.158 47.070 50.303 1.00 38.54 B ATOM 1165 CG LEU B 284 64.620 46.663 48.913 1.00 40.73 B ATOM 1166 CO1 LEU B 284 65.953 45.935 49.085 1.00 41.39 B ATOM 1167 CD2 LEU B 284 63.598 45.746 48.237 1.00 39.81 B ATOM 1168 C LEU B 284 62.331 47.606 51.903 1.00 37.57 B ATOM 1169 O LEU B 284 61.731 46.629 52.333 1.00 37.16 B ATOM 1170 N LYS B 285 62.654 48.636 52.679 1.00 37.42 B ATOM 1171 CA LYS B 285 62.258 48.638 54.071 1.00 37.32 B ATOM 1172 CB LYS B 285 62.706 49.927 54.757 1.00 37.90 B ATOM 1173 CG LYS B 285 64.221 50.101 54.711 1.00 41.29 B ATOM 1174 CD LYS B 285 64.714 51.417 55.305 1.00 43.06 B ATOM 1175 CE LYS B 285 64.504 51.487 56.811 1.00 44.78 B ATOM 1176 NZ LYS B 285 63.347 52.365 57.139 1.00 44.95 B ATOM 1177 C LYS B 285 60.754 48.531 54.078 1.00 36.58 B ATOM 1178 O LYS B 285 60.170 47.774 54.859 1.00 36.75 B ATOM 1179 N ILE B 286 60.137 49.268 53.163 1.00 34.81 B ATOM 1180 CA ILE B 286 58.687 49.286 53.038 1.00 34.65 B ATOM 1181 CB ILE B 286 58.233 50.340 51.988 1.00 35.18 B ATOM 1182 CG2 ILE B 286 56.723 50.435 51.961 1.00 34.75 B ATOM 1183 CG1 ILE B 286 58.778 51.721 52.361 1.00 36.78 B ATOM 1184 CD1 ILE B 286 58.517 52.777 51.304 1.00 35.35 B ATOM 1185 C ILE B 286 58.141 47.909 52.646 1.00 34.49 B ATOM 1186 O ILE B 286 57.109 47.469 53.163 1.00 34.87 B ATOM 1187 N PHE B 287 58.825 47.232 51.726 1.00 32.88 B ATOM 1188 CA PHE B 287 58.373 45.915 51.300 1.00 30.31 B ATOM 1189 CB PHE B 287 59.086 45.501 50.002 1.00 26.38 B ATOM 1190 CG PHE B 287 58.530 46.184 48.785 1.00 23.19 B ATOM 1191 CD1 PHE B 287 57.189 46.000 48.444 1.00 21.80 B ATOM 1192 CD2 PHE B 287 59.300 47.078 48.043 1.00 20.28 B ATOM 1193 CE1 PHE B 287 56.617 46.699 47.397 1.00 21.72 B ATOM 1194 CE2 PHE B 287 58.740 47.788 46.985 1.00 21.62 B ATOM 1195 CZ PHE B 287 57.389 47.599 46.659 1.00 23.65 B ATOM 1196 C PHE B 287 58.566 44.899 52.419 1.00 31.61 B ATOM 1197 O PHE B 287 57.864 43.887 52.487 1.00 32.92 B ATOM 1198 N ASN B 288 59.498 45.191 53.320 1.00 32.92 B ATOM 1199 CA ASN B 288 59.747 44.316 54.460 1.00 34.33 B ATOM 1200 CB ASN B 288 61.117 44.574 55.067 1.00 34.27 B ATOM 1201 CG ASN B 288 62.228 43.993 54.243 1.00 35.15 B ATOM 1202 OD1 ASN B 288 62.325 42.768 54.077 1.00 34.77 B ATOM 1203 ND2 ASN B 288 63.086 44.865 53.717 1.00 37.02 B ATOM 1204 C ASN B 288 58.699 44.515 55.538 1.00 34.60 B ATOM 1205 O ASN B 288 58.700 43.801 56.537 1.00 35.55 B ATOM 1206 N TYR B 289 57.833 45.507 55.347 1.00 33.60 B ATOM 1207 CA TYR B 289 56.757 45.786 56.286 1.00 32.28 B ATOM 1208 CB TYR B 289 56.597 47.288 56.536 1.00 30.88 B ATOM 1209 CG TYR B 289 57.639 47.906 57.444 1.00 31.04 B ATOM 1210 CD1 TYR B 289 57.824 47.445 58.743 1.00 29.76 B ATOM 1211 CE1 TYR B 289 58.783 48.005 59.577 1.00 28.80 B ATOM 1212 CD2 TYR B 289 58.441 48.954 57.001 1.00 30.42 B ATOM 1213 CE2 TYR B 289 59.404 49.520 57.828 1.00 30.11 B ATOM 1214 CZ TYR B 289 59.572 49.036 59.117 1.00 29.29 B ATOM 1215 OH TYR B 289 60.550 49.565 59.927 1.00 27.49 B ATOM 1216 C TYR B 289 55.454 45.259 55.712 1.00 33.20 B ATOM 1217 O TYR B 289 54.381 45.681 56.131 1.00 34.61 B ATOM 1218 N LEU B 290 55.538 44.348 54.750 1.00 32.98 B ATOM 1219 CA LEU B 290 54.335 43.794 54.148 1.00 33.98 B ATOM 1220 CB LEU B 290 54.181 44.325 52.736 1.00 33.99 B ATOM 1221 CG LEU B 290 53.894 45.813 52.594 1.00 34.25 B ATOM 1222 CD1 LEU B 290 53.690 46.102 51.123 1.00 32.35 B ATOM 1223 CD2 LEU B 290 52.629 46.192 53.393 1.00 35.31 B ATOM 1224 C LEU B 290 54.340 42.284 54.112 1.00 35.59 B ATOM 1225 O LEU B 290 55.366 41.686 53.832 1.00 37.73 B ATOM 1226 N GLN B 291 53.200 41.660 54.390 1.00 36.68 B ATOM 1227 CA GLN B 291 53.126 40.198 54.364 1.00 37.99 B ATOM 1228 CB GLN B 291 51.808 39.715 54.956 1.00 39.90 B ATOM 1229 CGG LN B 291 51.514 40.243 56.338 1.00 42.72 B ATOM 1230 CD GLN B 291 50.510 39.378 57.067 1.00 45.38 B ATOM 1231 OE1 GLN B 291 49.376 39.196 56.609 1.00 45.17 B ATOM 1232 NE2 GLN B 291 50.925 38.824 58.209 1.00 48.06 B ATOM 1233 C GLN B 291 53.254 39.696 52.937 1.00 37.97 B ATOM 1234 O GLN B 291 52.727 40.304 52.005 1.00 37.21 B ATOM 1235 N PHE B 292 53.924 38.566 52.769 1.00 39.53 B ATOM 1236 CA PHE B 292 54.154 38.038 51.430 1.00 42.10 B ATOM 1237 CB PHE B 292 54.592 36.565 51.510 1.00 43.75 B ATOM 1238 CG PHE B 292 53.463 35.605 51.727 1.00 44.90 B ATOM 1239 CD1 PHE B 292 52.799 35.038 50.641 1.00 43.90 B ATOM 1240 CD2 PHE B 292 53.050 35.280 53.014 1.00 45.10 B ATOM 1241 CE1 PHE B 292 51.742 34.161 50.831 1.00 43.67 B ATOM 1242 CE2 PHE B 292 51.992 34.403 53.217 1.00 44.65 B ATOM 1243 CZ PHE B 292 51.336 33.842 52.121 1.00 44.41 B ATOM 1244 C PHE B 292 52.990 38.217 50.441 1.00 42.01 B ATOM 1245 O PHE B 292 53.214 38.553 49.280 1.00 43.29 B ATOM 1246 N GLU B 293 51.753 38.018 50.884 1.00 41.02 B ATOM 1247 CA GLU B 293 50.605 38.176 49.985 1.00 40.82 B ATOM 1248 CB GLU B 293 49.289 38.028 50.769 1.00 41.39 B ATOM 1249 CG GLU B 293 49.056 36.617 51.350 1.00 42.89 B ATOM 1250 CD GLU B 293 49.451 36.480 52.818 1.00 43.53 B ATOM 1251 OE1 GLU B 293 50.507 37.006 53.222 1.00 44.09 B ATOM 1252 OE2 GLU B 293 48.704 35.825 53.572 1.00 45.55 B ATOM 1253 C GLU B 293 50.641 39.524 49.258 1.00 40.05 B ATOM 1254 O GLU B 293 50.375 39.603 48.056 1.00 38.85 B ATOM 1255 N ASP B 294 50.991 40.573 50.000 1.00 40.23 B ATOM 1256 CA ASP B 294 51.074 41.923 49.450 1.00 40.33 B ATOM 1257 CB ASP B 294 51.198 42.958 50.579 1.00 41.12 B ATOM 1258 CG ASP B 294 49.949 43.030 51.464 1.00 42.16 B ATOM 1259 OD1 ASP B 294 48.815 42.987 50.925 1.00 43.30 B ATOM 1260 OD2 ASP B 294 50.099 43.150 52.699 1.00 41.57 B ATOM 1261 C ASP B 294 52.259 42.074 48.490 1.00 38.83 B ATOM 1262 O ASP B 294 52.151 42.714 47.446 1.00 37.73 B ATOM 1263 N ILE B 295 53.390 41.477 48.840 1.00 37.53 B ATOM 1264 CA ILE B 295 54.561 41.573 47.994 1.00 36.43 B ATOM 1265 CB ILE B 295 55.751 40.853 48.638 1.00 35.75 B ATOM 1266 CG2 ILE B 295 56.926 40.801 47.660 1.00 35.40 B ATOM 1267 CG1 ILE B 295 56.107 41.574 49.950 1.00 36.24 B ATOM 1268 CD1 ILE B 295 57.303 41.033 50.709 1.00 36.08 B ATOM 1269 C ILE B 295 54.257 40.987 46.623 1.00 36.37 B ATOM 1270 O ILE B 295 54.707 41.504 45.593 1.00 36.01 B ATOM 1271 N ILE B 296 53.470 39.919 46.616 1.00 36.36 B ATOM 1272 CA ILE B 296 53.094 39.262 45.375 1.00 36.96 B ATOM 1273 CB ILE B 296 52.329 37.967 45.665 1.00 37.13 B ATOM 1274 CG2 ILE B 296 51.771 37.366 44.389 1.00 37.11 B ATOM 1275 CG1 ILE B 296 53.276 36.961 46.288 1.00 36.41 B ATOM 1276 CD1 ILE B 296 52.601 35.679 46.620 1.00 38.88 B ATOM 1277 C ILE B 296 52.256 40.159 44.473 1.00 36.89 B ATOM 1278 O ILE B 296 52.554 40.297 43.293 1.00 37.07 B ATOM 1279 N ASN B 297 51.208 40.769 45.008 1.00 37.95 B ATOM 1280 CA ASN B 297 50.385 41.649 44.186 1.00 38.86 B ATOM 1281 CB ASN B 297 49.240 42.246 44.980 1.00 41.69 B ATOM 1282 CG ASN B 297 48.368 41.213 45.583 1.00 43.05 B ATOM 1283 OD1 ASN B 297 47.914 40.293 44.897 1.00 44.19 B ATOM 1284 ND2 ASN B 297 48.114 41.345 46.880 1.00 43.88 B ATOM 1285 C ASN B 297 51.207 42.810 43.705 1.00 37.72 B ATOM 1286 O ASN B 297 50.953 43.360 42.632 1.00 36.87 B ATOM 1287 N SER B 298 52.167 43.207 44.531 1.00 36.60 B ATOM 1288 CA SER B 298 53.006 44.339 44.194 1.00 35.31 B ATOM 1289 CB SER B 298 53.926 44.673 45.366 1.00 32.10 B ATOM 1290 OG SER B 298 53.156 45.195 46.435 1.00 29.27 B ATOM 1291 C SER B 298 53.784 44.022 42.939 1.00 35.81 B ATOM 1292 O SER B 298 54.037 44.901 42.111 1.00 35.32 B ATOM 1293 N LEU B 299 54.136 42.750 42.793 1.00 36.25 B ATOM 1294 CA LEU B 299 54.871 42.291 41.625 1.00 36.42 B ATOM 1295 CB LEU B 299 55.218 40.814 41.771 1.00 35.83 B ATOM 1296 CG LEU B 299 56.431 40.528 42.654 1.00 36.52 B ATOM 1297 CD1 LEU B 299 56.674 39.028 42.727 1.00 37.64 B ATOM 1298 CD2 LEU B 299 57.655 41.224 42.065 1.00 35.78 B ATOM 1299 C LEU B 299 54.082 42.509 40.343 1.00 36.00 B ATOM 1300 O LEU B 299 54.660 42.539 39.256 1.00 36.92 B ATOM 1301 N CLY B 300 52.769 42.678 40.474 1.00 35.04 B ATOM 1302 CA GLY B 300 51.940 42.890 39.303 1.00 35.67 B ATOM 1303 C GLY B 300 51.417 44.305 39.186 1.00 35.69 B ATOM 1304 O GLY B 300 50.538 44.602 38.379 1.00 35.37 B ATOM 1305 N VAL B 301 51.958 45.194 39.998 1.00 36.32 B ATOM 1306 CA VAL B 301 51.523 46.569 39.969 1.00 36.62 B ATOM 1307 CB VAL B 301 51.953 47.291 41.247 1.00 37.56 B ATOM 1308 CG1 VAL B 301 51.752 48.789 41.087 1.00 37.50 B ATOM 1309 CG2 VAL B 301 51.133 46.752 42.436 1.00 35.20 B ATOM 1310 C VAL B 301 52.071 47.288 38.751 1.00 36.72 B ATOM 1311 O VAL B 301 51.321 47.910 38.017 1.00 37.30 B ATOM 1312 N SER B 302 53.378 47.201 38.534 1.00 37.60 B ATOM 1313 CA SER B 302 54.005 47.844 37.382 1.00 37.90 B ATOM 1314 CB SER B 302 54.317 49.311 37.684 1.00 37.39 B ATOM 1315 OG SER B 302 55.530 49.417 38.419 1.00 36.20 B ATOM 1316 C SER B 302 55.316 47.129 37.067 1.00 39.64 B ATOM 1317 O SER B 302 55.867 46.392 37.901 1.00 38.64 B ATOM 1318 N GLN B 303 55.821 47.371 35.861 1.00 40.39 B ATOM 1319 CA GLN B 303 57.087 46.781 35.428 1.00 41.46 B ATOM 1320 CB GLN B 303 57.436 47.239 34.013 1.00 41.20 B ATOM 1321 CG GLN B 303 56.696 46.481 32.950 1.00 43.64 B ATOM 1322 CD GLN B 303 57.199 45.068 32.815 1.00 44.54 B ATOM 1323 OE1 GLN B 303 57.771 44.517 33.751 1.00 46.50 B ATOM 1324 NE2 GLN B 303 56.986 44.466 31.650 1.00 44.23 B ATOM 1325 C GLN B 303 58.241 47.140 36.360 1.00 41.74 B ATOM 1326 O GLN B 303 59.163 46.345 36.561 1.00 41.80 B ATOM 1327 N ASN B 304 58.194 48.338 36.928 1.00 42.15 B ATOM 1328 CA ASN B 304 59.251 48.758 37.826 1.00 41.69 B ATOM 1329 CB ASN B 304 59.237 50.263 38.014 1.00 43.58 B ATOM 1330 CG ASN B 304 60.623 50.861 37.924 1.00 45.74 B ATOM 1331 OD1 ASN B 304 61.599 50.302 38.459 1.00 46.54 B ATOM 1332 ND2 ASN B 304 60.728 52.009 37.240 1.00 47.34 B ATOM 1333 G ASN B 304 59.130 48.100 39.174 1.00 41.16 B ATOM 1334 O ASN B 304 60.126 47.650 39.739 1.00 40.69 B ATOM 1335 N TRP B 305 57.910 48.060 39.700 1.00 40.22 B ATOM 1336 CA TRP B 305 57.687 47.439 40.992 1.00 39.44 B ATOM 1337 CB TRP B 305 56.201 47.464 41.357 1.00 40.05 B ATOM 1338 CG TRP B 305 55.742 48.762 41.945 1.00 41.46 B ATOM 1339 CD2 TRP B 305 54.933 48.939 43.120 1.00 42.85 B ATOM 1340 CE2 TRP B 305 54.724 50.324 43.277 1.00 43.18 B ATOM 1341 CE3 TRP B 305 54.363 48.060 44.054 1.00 43.70 B ATOM 1342 CD1 TRP B 305 55.983 50.007 41.456 1.00 41.95 B ATOM 1343 NE1 TRP B 305 55.375 50.953 42.248 1.00 43.45 B ATOM 1344 CZ2 TRP B 305 53.966 50.858 44.336 1.00 43.29 B ATOM 1345 CZ3 TRP B 305 53.608 48.591 45.108 1.00 43.59 B ATOM 1346 CH2 TRP B 305 53.419 49.976 45.237 1.00 43.13 B ATOM 1347 C TRP B 305 58.186 46.007 40.930 1.00 39.39 B ATOM 1348 O TRP B 305 58.909 45.556 41.818 1.00 40.05 B ATOM 1349 N ASN B 306 57.808 45.300 39.868 1.00 38.31 B ATOM 1350 CA ASN B 306 58.213 43.915 39.699 1.00 36.89 B ATOM 1351 CB ASN B 306 57.558 43.318 38.449 1.00 39.69 B ATOM 1352 CG ASN B 306 57.874 41.836 38.265 1.00 41.87 B ATOM 1353 OD1 ASN B 306 58.898 41.465 37.690 1.00 42.36 B ATOM 1354 ND2 ASN B 306 56.989 40.983 38.763 1.00 44.37 B ATOM 1355 C ASN B 306 59.730 43.817 39.608 1.00 35.41 B ATOM 1356 O ASN B 306 60.333 42.902 40.170 1.00 35.33 B ATOM 1357 N LYS B 307 60.353 44.765 38.917 1.00 34.02 B ATOM 1358 CA LYS B 307 61.804 44.750 38.786 1.00 34.18 B ATOM 1359 CB LYS B 307 62.245 45.720 37.686 1.00 34.16 B ATOM 1360 CG LYS B 307 63.753 45.889 37.572 1.00 34.46 B ATOM 1361 CD LYS B 307 64.121 46.934 36.524 1.00 36.66 B ATOM 1362 CE LYS B 307 63.783 46.479 35.089 1.00 39.17 B ATOM 1363 NZ LYS B 307 62.308 46.327 34.816 1.00 41.27 B ATOM 1364 C LYS B 307 62.491 45.096 40.110 1.00 34.15 B ATOM 1365 O LYS B 307 63.484 44.476 40.486 1.00 35.79 B ATOM 1366 N ILE B 308 61.967 46.089 40.814 1.00 33.56 B ATOM 1367 CA ILE B 308 62.539 46.483 42.090 1.00 32.11 B ATOM 1368 CB ILE B 308 61.790 47.706 42.670 1.00 31.25 B ATOM 1369 CG2 ILE B 308 62.235 47.954 44.118 1.00 29.28 B ATOM 1370 CG1 ILE B 308 62.010 48.918 41.746 1.00 30.74 B ATOM 1371 CD1 ILE B 308 61.163 50.148 42.057 1.00 30.81 B ATOM 1372 C ILE B 308 62.455 45.330 43.083 1.00 32.53 B ATOM 1373 O ILE B 308 63.432 44.996 43.741 1.00 33.24 B ATOM 1374 N ILE B 309 61.288 44.706 43.174 1.00 32.71 B ATOM 1375 CA ILE B 309 61.094 43.616 44.120 1.00 32.29 B ATOM 1376 CB ILE B 309 59.605 43.255 44.224 1.00 31.48 B ATOM 1377 CG2 ILE B 309 59.436 41.944 44.993 1.00 28.42 B ATOM 1378 CG1 ILE B 309 58.860 44.419 44.894 1.00 29.43 B ATOM 1379 CD1 ILE B 309 57.377 44.244 45.030 1.00 29.32 B ATOM 1380 C ILE B 309 61.881 42.360 43.801 1.00 32.95 B ATOM 1381 O ILE B 309 62.297 41.616 44.705 1.00 33.10 B ATOM 1382 N ARG B 310 62.088 42.120 42.515 1.00 32.48 B ATOM 1383 CA ARG B 310 62.807 40.929 42.113 1.00 31.41 B ATOM 1384 CB ARG B 310 62.401 40.562 40.701 1.00 30.53 B ATOM 1385 CG ARG B 310 61.047 39.954 40.749 1.00 32.30 B ATOM 1386 CD ARG B 310 60.974 38.823 39.812 1.00 33.94 B ATOM 1387 NE ARG B 310 60.659 39.310 38.485 1.00 36.53 B ATOM 1388 CZ ARG B 310 60.989 38.682 37.369 1.00 37.75 B ATOM 1389 NH1 ARG B 310 61.656 37.535 37.428 1.00 36.97 B ATOM 1390 NH2 ARG B 310 60.649 39.205 36.200 1.00 38.45 B ATOM 1391 C ARG B 310 64.302 41.065 42.259 1.00 30.16 B ATOM 1392 O ARG B 310 65.059 40.091 42.152 1.00 28.61 B ATOM 1393 N LYS B 311 64.717 42.283 42.552 1.00 29.95 B ATOM 1394 CA LYS B 311 66.122 42.542 42.727 1.00 31.78 B ATOM 1395 CB LYS B 311 66.419 44.014 42.471 1.00 30.98 B ATOM 1396 CG LYS B 311 67.876 44.355 42.676 1.00 34.65 B ATOM 1397 CD LYS B 311 68.141 45.839 42.539 0.00 34.39 B ATOM 1398 CE LYS B 311 68.033 46.305 41.095 0.00 35.04 B ATOM 1399 NZ LYS B 311 66.665 46.176 40.520 0.00 35.23 B ATOM 1400 C LYS B 311 66.589 42.154 44.127 1.00 31.89 B ATOM 1401 O LYS B 311 67.761 41.815 44.325 1.00 31.11 B ATOM 1402 N SER B 312 65.666 42.181 45.088 1.00 32.44 B ATOM 1403 CA SER B 312 65.997 41.868 46.479 1.00 34.40 B ATOM 1404 CB SER B 312 64.998 42.541 47.433 1.00 35.97 B ATOM 1405 OG SER B 312 65.318 42.268 48.793 1.00 37.24 B ATOM 1406 C SER B 312 66.068 40.389 46.825 1.00 33.58 B ATOM 1407 O SER B 312 65.154 39.629 46.532 1.00 35.14 B ATOM 1408 N THR B 313 67.160 39.990 47.460 1.00 32.17 B ATOM 1409 CA THR B 313 67.314 38.613 47.867 1.00 32.11 B ATOM 1410 CB THR B 313 68.760 38.142 47.682 1.00 34.02 B ATOM 1411 OG1 THR B 313 68.921 37.648 46.346 1.00 35.15 B ATOM 1412 CG2 THR B 313 69.114 37.055 48.685 1.00 33.55 B ATOM 1413 C THR B 313 66.913 38.532 49.329 1.00 30.50 B ATOM 1414 O THR B 313 66.318 37.553 49.764 1.00 31.15 B ATOM 1415 N SER B 314 67.219 39.583 50.078 1.00 29.28 B ATOM 1416 CA SER B 314 66.881 39.648 51.493 1.00 28.64 B ATOM 1417 CB SER B 314 67.307 40.990 52.076 1.00 28.48 B ATOM 1418 OG SER B 314 68.696 40.979 52.349 1.00 33.47 B ATOM 1419 C SER B 314 65.397 39.479 51.710 1.00 27.68 B ATOM 1420 O SER B 314 64.966 38.738 52.592 1.00 28.00 B ATOM 1421 N LEU B 315 64.629 40.182 50.890 1.00 25.95 B ATOM 1422 CA LEU B 315 63.190 40.158 50.967 1.00 24.83 B ATOM 1423 CB LEU B 315 62.614 40.721 49.676 1.00 22.38 B ATOM 1424 CG LEU B 315 61.151 41.129 49.740 1.00 21.41 B ATOM 1425 CD1 LEU B 315 61.006 42.400 50.604 1.00 20.01 B ATOM 1426 CD2 LEU B 315 60.662 41.376 48.345 1.00 19.89 B ATOM 1427 C LEU B 315 62.675 38.745 51.206 1.00 26.71 B ATOM 1428 O LEU B 315 61.894 38.494 52.141 1.00 27.54 B ATOM 1429 N TRP B 316 63.110 37.813 50.369 1.00 26.88 B ATOM 1430 CA TRP B 316 62.665 36.439 50.534 1.00 27.42 B ATOM 1431 CB TRP B 316 62.776 35.691 49.204 1.00 27.04 B ATOM 1432 CG TRP B 316 62.021 36.416 48.176 1.00 25.52 B ATOM 1433 CD2 TRP B 316 60.600 36.519 48.088 1.00 25.34 B ATOM 1434 CE2 TRP B 316 60.313 37.456 47.071 1.00 24.36 B ATOM 1435 CE3 TRP B 316 59.540 35.920 48.778 1.00 26.16 B ATOM 1436 CD1 TRP B 316 62.526 37.262 47.232 1.00 25.54 B ATOM 1437 NE1 TRP B 316 61.507 37.892 46.566 1.00 23.85 B ATOM 1438 CZ2 TRP B 316 59.003 37.808 46.728 1.00 23.50 B ATOM 1439 CZ3 TRP B 316 58.236 36.272 48.438 1.00 24.82 B ATOM 1440 CH2 TRP B 316 57.981 37.209 47.421 1.00 24.99 B ATOM 1441 C TRP B 316 63.402 35.720 51.656 1.00 27.65 B ATOM 1442 O TRP B 316 62.786 34.989 52.446 1.00 27.76 B ATOM 1443 N LYS B 317 64.709 35.934 51.744 1.00 27.10 B ATOM 1444 CA LYS B 317 65.455 35.304 52.817 1.00 28.92 B ATOM 1445 CB LYS B 317 66.907 35.788 52.830 1.00 30.51 B ATOM 1446 CG LYS B 317 67.768 35.175 53.935 1.00 32.68 B ATOM 1447 CD LYS B 317 69.209 35.655 53.820 1.00 35.89 B ATOM 1448 CE LYS B 317 69.849 35.839 55.186 1.00 37.32 B ATOM 1449 NZ LYS B 317 69.169 36.927 55.978 1.00 39.48 B ATOM 1450 C LYS B 317 64.764 35.597 54.164 1.00 29.21 B ATOM 1451 O LYS B 317 64.560 34.682 54.975 1.00 28.72 B ATOM 1452 N LYS B 318 64.373 36.851 54.394 1.00 27.41 B ATOM 1453 CA LYS B 318 63.698 37.182 55.640 1.00 27.23 B ATOM 1454 CB LYS B 318 63.287 38.657 55.685 1.00 28.22 B ATOM 1455 CG LYS B 318 64.448 39.580 55.982 1.00 29.33 B ATOM 1456 CD LYS B 318 64.011 40.989 56.263 1.00 29.29 B ATOM 1457 CE LYS B 318 65.211 41.805 56.726 1.00 31.20 B ATOM 1458 NZ LYS B 318 66.332 41.748 55.749 1.00 29.62 B ATOM 1459 C LYS B 318 62.475 36.318 55.846 1.00 28.19 B ATOM 1460 O LYS B 318 62.325 35.651 56.881 1.00 29.19 B ATOM 1461 N LEU B 319 61.598 36.346 54.847 1.00 28.31 B ATOM 1462 CA LEU B 319 60.353 35.576 54.851 1.00 26.08 B ATOM 1463 CB LEU B 319 59.644 35.756 53.499 1.00 24.60 B ATOM 1464 CG LEU B 319 58.949 37.106 53.299 1.00 23.31 B ATOM 1465 CD1 LEU B 319 58.929 37.501 51.828 1.00 25.42 B ATOM 1466 CD2 LEU B 319 57.550 37.030 53.849 1.00 20.66 B ATOM 1467 C LEU B 319 60.661 34.104 55.115 1.00 24.68 B ATOM 1468 O LEU B 319 60.126 33.511 56.051 1.00 24.33 B ATOM 1469 N LEU B 320 61.521 33.515 54.292 1.00 24.37 B ATOM 1470 CA LEU B 320 61.887 32.119 54.496 1.00 24.33 B ATOM 1471 CB LEU B 320 63.119 31.777 53.678 1.00 20.97 B ATOM 1472 CG LEU B 320 62.711 31.425 52.272 1.00 20.93 B ATOM 1473 CD1 LEU B 320 63.945 31.333 51.431 1.00 21.63 B ATOM 1474 CD2 LEU B 320 61.936 30.117 52.276 1.00 17.66 B ATOM 1475 C LEU B 320 62.166 31.800 55.967 1.00 24.55 B ATOM 1476 O LEU B 320 61.744 30.769 56.491 1.00 25.31 B ATOM 1477 N ILE B 321 62.883 32.706 56.615 1.00 24.47 B ATOM 1478 CA ILE B 321 63.253 32.579 58.009 1.00 23.96 B ATOM 1479 CB ILE B 321 64.450 33.531 58.315 1.00 25.52 B ATOM 1480 CG2 ILE B 321 64.759 33.556 59.806 1.00 25.19 B ATOM 1481 CG1 ILE B 321 65.671 33.094 57.498 1.00 23.92 B ATOM 1482 CD1 ILE B 321 66.951 33.873 57.782 1.00 24.41 B ATOM 1483 C ILE B 321 62.065 32.882 58.928 1.00 23.22 B ATOM 1484 O ILE B 321 61.902 32.240 59.952 1.00 24.18 B ATOM 1485 N SER B 322 61.239 33.853 58.563 1.00 23.04 B ATOM 1486 CA SER B 322 60.079 34.200 59.370 1.00 23.65 B ATOM 1487 CB SER B 322 59.248 35.266 58.670 1.00 21.62 B ATOM 1488 OG SER B 322 60.030 36.403 58.387 1.00 24.32 B ATOM 1489 C SER B 322 59.203 32.990 59.581 1.00 24.95 B ATOM 1490 O SER B 322 58.789 32.691 60.696 1.00 28.00 B ATOM 1491 N GLD B 323 58.926 32.302 58.485 1.00 25.30 B ATOM 1492 CA GLD B 323 58.066 31.135 58.486 1.00 25.97 B ATOM 1493 CB GLD B 323 57.480 30.974 57.091 1.00 26.35 B ATOM 1494 CG GLD B 323 56.792 32.239 56.646 1.00 27.43 B ATOM 1495 CD GLD B 323 55.441 32.431 57.307 1.00 27.80 B ATOM 1496 OE1 GLD B 323 55.239 31.878 58.409 1.00 25.90 B ATOM 1497 OE2 GLD B 323 54.590 33.142 56.718 1.00 28.13 B ATOM 1498 C GLD B 323 58.745 29.855 58.917 1.00 25.13 B ATOM 1499 O GLD B 323 58.123 28.792 58.931 1.00 25.20 B ATOM 1500 N ASN B 324 60.019 29.966 59.276 1.00 24.08 B ATOM 1501 CA ASN B 324 60.808 28.816 59.708 1.00 24.96 B ATOM 1502 CB ASN B 324 60.203 28.185 60.974 1.00 26.02 B ATOM 1503 CG ASN B 324 60.051 29.187 62.108 1.00 28.82 B ATOM 1504 OD1 ASN B 324 61.030 29.766 62.605 1.00 29.61 B ATOM 1505 ND2 ASN B 324 58.813 29.402 62.518 1.00 29.76 B ATOM 1506 C ASN B 324 60.906 27.776 58.588 1.00 24.92 B ATOM 1507 O ASN B 324 60.642 26.596 58.786 1.00 23.18 B ATOM 1508 N PHE B 325 61.269 28.226 57.395 1.00 25.71 B ATOM 1509 CA PHE B 325 61.406 27.304 56.287 1.00 25.91 B ATOM 1510 CB PHE B 325 60.839 27.913 55.008 1.00 24.25 B ATOM 1511 CG PHE B 325 59.334 27.935 54.987 1.00 23.73 B ATOM 1512 CD1 PHE B 325 58.644 28.984 54.394 1.00 23.04 B ATOM 1513 CD2 PHE B 325 58.604 26.925 55.616 1.00 20.21 B ATOM 1514 CE1 PHE B 325 57.259 29.025 54.437 1.00 20.96 B ATOM 1515 CE2 PHE B 325 57.227 26.964 55.658 1.00 18.74 B ATOM 1516 CZ PHE B 325 56.555 28.015 55.073 1.00 19.51 B ATOM 1517 C PHE B 325 62.861 26.972 56.156 1.00 26.92 B ATOM 1518 O PHE B 325 63.232 26.019 55.478 1.00 28.62 B ATOM 1519 N VAL B 326 63.683 27.766 56.833 1.00 27.50 B ATOM 1520 CA VAL B 326 65.127 27.577 56.849 1.00 27.18 B ATOM 1521 CB VAL B 326 65.773 28.060 55.532 1.00 25.75 B ATOM 1522 CG1 VAL B 326 66.019 29.553 55.587 1.00 23.02 B ATOM 1523 CG2 VAL B 326 67.061 27.316 55.288 1.00 26.04 B ATOM 1524 C VAL B 326 65.685 28.408 57.993 1.00 28.22 B ATOM 1525 O VAL B 326 64.998 29.274 58.533 1.00 28.23 B ATOM 1526 N SER B 327 66.932 28.154 58.361 1.00 29.87 B ATOM 1527 CA SER B 327 67.547 28.926 59.427 1.00 32.04 B ATOM 1528 CB SER B 327 67.867 28.053 60.643 1.00 32.92 B ATOM 1529 OG SER B 327 69.012 27.244 60.404 1.00 35.60 B ATOM 1530 C SER B 327 68.837 29.511 58.905 1.00 33.44 B ATOM 1531 O SER B 327 69.404 29.024 57.925 1.00 35.13 B ATOM 1532 N PRO B 328 69.328 30.561 59.568 1.00 34.95 B ATOM 1533 CD PRO B 328 68.703 31.277 60.698 1.00 34.72 B ATOM 1534 CA PRO B 328 70.570 31.208 59.161 1.00 35.43 B ATOM 1535 CB PRO B 328 70.906 32.056 60.372 1.00 34.44 B ATOM 1536 CG PRO B 328 69.541 32.530 60.792 1.00 34.00 B ATOM 1537 C PRO B 328 71.674 30.211 58.789 1.00 37.33 B ATOM 1538 O PRO B 328 72.413 30.428 57.820 1.00 38.07 B ATOM 1539 N LYS B 329 71.779 29.106 59.524 1.00 38.13 B ATOM 1540 CA LYS B 329 72.830 28.126 59.222 1.00 39.44 B ATOM 1541 CB LYS B 329 73.088 27.201 60.423 1.00 41.96 B ATOM 1542 CG LYS B 329 73.334 27.911 61.736 1.00 44.54 B ATOM 1543 CD LYS B 329 74.564 28.801 61.693 1.00 46.08 B ATOM 1544 CE LYS B 329 74.745 29.475 63.047 1.00 47.88 B ATOM 1545 NZ LYS B 329 73.510 30.241 63.384 1.00 48.71 B ATOM 1546 C LYS B 329 72.539 27.255 58.005 1.00 38.23 B ATOM 1547 O LYS B 329 73.444 26.922 57.230 1.00 37.43 B ATOM 1548 N GLY B 330 71.279 26.863 57.858 1.00 36.83 B ATOM 1549 CA GLY B 330 70.904 26.026 56.733 1.00 34.91 B ATOM 1550 C GLY B 330 70.671 26.809 55.458 1.00 33.34 B ATOM 1551 O GLY B 330 70.432 26.217 54.402 1.00 31.96 B ATOM 1552 N PHE B 331 70.742 28.136 55.554 1.00 32.27 B ATOM 1553 CA PHE B 331 70.517 28.977 54.388 1.00 32.81 B ATOM 1554 CB PHE B 331 70.778 30.454 54.688 1.00 32.71 B ATOM 1555 CG PHE B 331 70.365 31.374 53.561 1.00 35.02 B ATOM 1556 CD1 PHE B 331 69.013 31.631 53.319 1.00 34.88 B ATOM 1557 CD2 PHE B 331 71.323 31.971 52.727 1.00 36.79 B ATOM 1558 CE1 PHE B 331 68.609 32.466 52.274 1.00 35.03 B ATOM 1559 CE2 PHE B 331 70.933 32.816 51.670 1.00 36.82 B ATOM 1560 CZ PHE B 331 69.568 33.061 51.446 1.00 36.85 B ATOM 1561 C PHE B 331 71.333 28.600 53.164 1.00 32.72 B ATOM 1562 O PHE B 331 70.779 28.197 52.143 1.00 32.53 B ATOM 1563 N ASN B 332 72.650 28.725 53.261 1.00 33.63 B ATOM 1564 CA ASN B 332 73.495 28.430 52.116 1.00 34.96 B ATOM 1565 CB ASN B 332 74.956 28.510 52.503 1.00 35.07 B ATOM 1566 CG ASN B 332 75.386 29.925 52.769 1.00 36.45 B ATOM 1567 OD1 ASN B 332 74.860 30.864 52.165 1.00 36.09 B ATOM 1568 ND2 ASN B 332 76.352 30.096 53.666 1.00 37.34 B ATOM 1569 C ASN B 332 73.204 27.105 51.457 1.00 35.37 B ATOM 1570 O ASN B 332 73.006 27.034 50.240 1.00 34.82 B ATOM 1571 N SER B 333 73.174 26.050 52.253 1.00 36.35 B ATOM 1572 CA SER B 333 72.897 24.749 51.696 1.00 38.23 B ATOM 1573 CB SER B 333 72.767 23.724 52.804 1.00 37.83 B ATOM 1574 OG SER B 333 72.509 22.458 52.236 1.00 43.08 B ATOM 1575 C SER B 333 71.615 24.785 50.867 1.00 38.81 B ATOM 1576 O SER B 333 71.522 24.144 49.814 1.00 39.26 B ATOM 1577 N LEU B 334 70.629 25.533 51.357 1.00 38.86 B ATOM 1578 CA LEU B 334 69.338 25.688 50.685 1.00 37.16 B ATOM 1579 CB LEU B 334 68.446 26.645 51.486 1.00 34.21 B ATOM 1580 CG LEU B 334 67.149 27.126 50.830 1.00 33.30 B ATOM 1581 CD1 LEU B 334 66.189 25.957 50.642 1.00 29.33 B ATOM 1582 CD2 LEU B 334 66.528 28.209 51.688 1.00 31.65 B ATOM 1583 C LEU B 334 69.574 26.251 49.291 1.00 37.44 B ATOM 1584 O LEU B 334 69.105 25.700 48.293 1.00 36.40 B ATOM 1585 N ASN B 335 70.306 27.361 49.248 1.00 38.10 B ATOM 1586 CA ASN B 335 70.647 28.032 48.001 1.00 38.02 B ATOM 1587 CB ASN B 335 71.590 29.188 48.289 1.00 37.88 B ATOM 1588 CG ASN B 335 70.871 30.496 48.329 1.00 40.34 B ATOM 1589 OD1 ASN B 335 71.266 31.422 49.033 1.00 43.76 B ATOM 1590 ND2 ASN B 335 69.800 30.591 47.556 1.00 41.28 B ATOM 1591 C ASN B 335 71.292 27.070 47.013 1.00 38.24 B ATOM 1592 O ASN B 335 70.906 27.003 45.847 1.00 38.64 B ATOM 1593 N LEU B 336 72.274 26.325 47.498 1.00 36.78 B ATOM 1594 CA LEU B 336 72.978 25.364 46.683 1.00 35.71 B ATOM 1595 CB LEU B 336 74.041 24.658 47.522 1.00 35.78 B ATOM 1596 CG LEU B 336 74.991 23.682 46.827 1.00 35.54 B ATOM 1597 CD1 LEU B 336 75.977 24.436 45.942 1.00 35.55 B ATOM 1598 CD2 LEU B 336 75.716 22.899 47.883 1.00 36.31 B ATOM 1599 C LEU B 336 71.997 24.336 46.123 1.00 35.77 B ATOM 1600 O LEU B 336 72.075 23.961 44.954 1.00 37.71 B ATOM 1601 N LYS B 337 71.068 23.876 46.953 1.00 34.49 B ATOM 1602 CA LYS B 337 70.097 22.878 46.508 1.00 31.85 B ATOM 1603 CB LYS B 337 69.310 22.320 47.704 1.00 30.25 B ATOM 1604 CG LYS B 337 68.298 21.237 47.321 1.00 32.14 B ATOM 1605 CD LYS B 337 67.438 20.697 48.512 1.00 35.02 B ATOM 1606 CE LYS B 337 66.544 21.789 49.173 1.00 35.41 B ATOM 1607 NZ LYS B 337 65.466 21.260 50.081 1.00 32.74 B ATOM 1608 C LYS B 337 69.129 23.433 45.461 1.00 30.95 B ATOM 1609 O LYS B 337 68.793 22.740 44.519 1.00 29.84 B ATOM 1610 N LEU B 338 68.690 24.679 45.636 1.00 31.30 B ATOM 1611 CA LEU B 338 67.755 25.324 44.714 1.00 30.02 B ATOM 1612 CB LEU B 338 67.218 26.621 45.317 1.00 29.04 B ATOM 1613 CG LEU B 338 66.157 26.563 46.434 1.00 29.18 B ATOM 1614 CD1 LEU B 338 65.834 27.996 46.909 1.00 25.48 B ATOM 1615 CD2 LEU B 338 64.897 25.881 45.919 1.00 26.03 B ATOM 1616 C LEU B 338 68.433 25.639 43.400 1.00 30.20 B ATOM 1617 O LEU B 338 67.809 25.643 42.340 1.00 29.78 B ATOM 1618 N SER B 339 69.724 25.918 43.487 1.00 30.16 B ATOM 1619 CA SER B 339 70.510 26.227 42.317 1.00 29.06 B ATOM 1620 CB SER B 339 71.913 26.656 42.712 1.00 27.05 B ATOM 1621 OG SER B 339 72.665 26.965 41.560 1.00 25.97 B ATOM 1622 C SER B 339 70.598 24.979 41.483 1.00 30.90 B ATOM 1623 O SER B 339 70.580 25.029 40.254 1.00 32.89 B ATOM 1624 N GLN B 340 70.701 23.842 42.149 1.00 30.57 B ATOM 1625 CA GLN B 340 70.796 22.605 41.409 1.00 31.13 B ATOM 1626 CB GLN B 340 71.238 21.496 42.334 1.00 32.53 B ATOM 1627 CG GLN B 340 72.619 21.768 42.867 1.00 35.89 B ATOM 1628 CD GLN B 340 73.040 20.758 43.900 1.00 36.30 B ATOM 1629 OE1 GLN B 340 72.209 19.975 44.393 1.00 37.07 B ATOM 1630 NE2 GLN B 340 74.332 20.765 44.248 1.00 34.68 B ATOM 1631 C GLN B 340 69.471 22.276 40.774 1.00 31.71 B ATOM 1632 O GLN B 340 69.418 21.644 39.726 1.00 32.80 B ATOM 1633 N LYS B 341 68.403 22.738 41.408 1.00 32.39 B ATOM 1634 CA LYS B 341 67.047 22.505 40.942 1.00 33.18 B ATOM 1635 CB LYS B 341 66.086 22.760 42.094 1.00 34.86 B ATOM 1636 CG LYS B 341 64.697 22.223 41.889 1.00 38.21 B ATOM 1637 CD LYS B 341 63.793 22.574 43.061 1.00 40.03 B ATOM 1638 CE LYS B 341 62.406 21.980 42.836 1.00 42.58 B ATOM 1639 NZ LYS B 341 61.380 22.609 43.719 1.00 42.83 B ATOM 1640 C LYS B 341 66.661 23.392 39.764 1.00 34.36 B ATOM 1641 O LYS B 341 66.041 22.939 38.805 1.00 34.14 B ATOM 1642 N TYR B 342 67.043 24.658 39.857 1.00 34.90 B ATOM 1643 CA TYR B 342 66.734 25.660 38.853 1.00 35.01 B ATOM 1644 CB TYR B 342 65.844 26.695 39.497 1.00 37.87 B ATOM 1645 CG TYR B 342 64.647 26.082 40.153 1.00 41.65 B ATOM 1646 CD1 TYR B 342 63.646 25.507 39.384 1.00 42.60 B ATOM 1647 CE1 TYR B 342 62.525 24.958 39.968 1.00 45.40 B ATOM 1648 CD2 TYR B 342 64.501 26.088 41.538 1.00 42.64 B ATOM 1649 CE2 TYR B 342 63.376 25.540 42.139 1.00 44.31 B ATOM 1650 CZ TYR B 342 62.386 24.978 41.343 1.00 45.73 B ATOM 1651 OH TYR B 342 61.232 24.462 41.896 1.00 46.50 B ATOM 1652 C TYR B 342 67.991 26.339 38.343 1.00 34.71 B ATOM 1653 O TYR B 342 68.287 27.467 38.729 1.00 35.57 B ATOM 1654 N PRO B 343 68.754 25.663 37.474 1.00 34.09 B ATOM 1655 CD PRO B 343 68.568 24.298 36.955 1.00 33.06 B ATOM 1656 CA PRO B 343 69.982 26.256 36.942 1.00 34.15 B ATOM 1657 CB PRO B 343 70.427 25.231 35.902 1.00 32.61 B ATOM 1658 CG PRO B 343 69.940 23.953 36.458 1.00 30.81 B ATOM 1659 C PRO B 343 69.805 27.655 36.332 1.00 34.54 B ATOM 1660 O PRO B 343 70.562 28.577 36.639 1.00 34.01 B ATOM 1661 N LYS B 344 68.793 27.803 35.483 1.00 34.28 B ATOM 1662 CA LYS B 344 68.537 29.063 34.799 1.00 34.41 B ATOM 1663 CB LYS B 344 67.823 28.791 33.483 1.00 34.70 B ATOM 1664 CG LYS B 344 68.487 27.758 32.623 1.00 32.84 B ATOM 1665 CD LYS B 344 67.566 27.409 31.505 1.00 32.13 B ATOM 1666 CE LYS B 344 67.769 25.984 31.078 1.00 32.95 B ATOM 1667 NZ LYS B 344 66.694 25.581 30.144 1.00 35.30 B ATOM 1668 C LYS B 344 67.778 30.156 35.547 1.00 34.52 B ATOM 1669 CD LYS B 344 67.446 31.188 34.950 1.00 33.51 B ATOM 1670 N LEU B 345 67.475 29.921 36.825 1.00 32.93 B ATOM 1671 CA LEU B 345 66.792 30.916 37.663 1.00 30.85 B ATOM 1672 CB LEU B 345 65.856 30.253 38.660 1.00 28.33 B ATOM 1673 CG LEU B 345 64.506 29.850 38.111 1.00 27.26 B ATOM 1674 CD1 LEU B 345 63.691 29.121 39.179 1.00 24.62 B ATOM 1675 CD2 LEU B 345 63.804 31.102 37.655 1.00 26.44 B ATOM 1676 C LEU B 345 67.834 31.674 38.440 1.00 31.07 B ATOM 1677 O LEU B 345 68.961 31.210 38.580 1.00 31.79 B ATOM 1678 N SER B 346 67.458 32.830 38.970 1.00 33.11 B ATOM 1679 CA SER B 346 68.392 33.653 39.754 1.00 34.10 B ATOM 1680 CB SER B 346 68.283 35.114 39.349 1.00 34.20 B ATOM 1681 OG SER B 346 67.035 35.623 39.779 1.00 37.09 B ATOM 1682 C SER B 346 68.098 33.563 41.247 1.00 33.12 B ATOM 1683 O SER B 346 66.971 33.302 41.655 1.00 33.78 B ATOM 1684 N GLN B 347 69.113 33.814 42.056 1.00 32.28 B ATOM 1685 CA GLN B 347 68.950 33.749 43.495 1.00 32.88 B ATOM 1686 CB GLN B 347 70.071 34.502 44.177 1.00 33.73 B ATOM 1687 CG GLN B 347 70.009 34.451 45.667 1.00 33.40 B ATOM 1688 CD GLN B 347 71.105 35.276 46.251 1.00 36.19 B ATOM 1689 OE1 GLN B 347 71.164 36.494 46.031 1.00 38.25 B ATOM 1690 NE2 GLN B 347 72.006 34.627 46.984 1.00 36.38 B ATOM 1691 C GLN B 347 67.620 34.314 43.973 1.00 31.82 B ATOM 1692 O GLN B 347 66.834 33.616 44.620 1.00 31.26 B ATOM 1693 N GLN B 348 67.370 35.581 43.661 1.00 30.61 B ATOM 1694 CA GLN B 348 66.121 36.195 44.076 1.00 30.85 B ATOM 1695 CB GLN B 348 65.984 37.626 43.542 1.00 31.61 B ATOM 1696 CG GLN B 348 67.092 38.583 43.958 1.00 31.41 B ATOM 1697 CD GLN B 348 68.291 38.552 43.014 1.00 30.33 B ATOM 1698 OE1 GLN B 348 69.055 39.512 42.942 1.00 29.04 B ATOM 1699 NE2 GLN B 348 68.461 37.452 42.296 1.00 29.86 B ATOM 1700 C GLN B 348 64.942 35.364 43.593 1.00 29.45 B ATOM 1701 O GLN B 348 64.183 34.831 44.400 1.00 28.92 B ATOM 1702 N ASP B 349 64.776 35.236 42.283 1.00 28.60 B ATOM 1703 CA ASP B 349 63.646 34.458 41.805 1.00 27.39 B ATOM 1704 CB ASP B 349 63.631 34.372 40.282 1.00 28.50 B ATOM 1705 CG ASP B 349 63.164 35.666 39.632 1.00 30.39 B ATOM 1706 OD1 ASP B 349 62.212 36.306 40.153 1.00 29.22 B ATOM 1707 OD2 ASP B 349 63.744 36.034 38.590 1.00 31.83 B ATOM 1708 C ASP B 349 63.571 33.061 42.404 1.00 25.37 B ATOM 1709 O ASP B 349 62.476 32.546 42.597 1.00 24.91 B ATOM 1710 N ARG B 350 64.720 32.454 42.695 1.00 22.81 B ATOM 1711 CA ARG B 350 64.746 31.117 43.280 1.00 21.59 B ATOM 1712 CB ARG B 350 66.178 30.611 43.428 1.00 23.28 B ATOM 1713 CG ARG B 350 66.787 30.106 42.133 1.00 27.24 B ATOM 1714 CD ARG B 350 68.195 29.544 42.333 1.00 26.74 B ATOM 1715 NE ARG B 350 68.820 29.271 41.051 1.00 27.71 B ATOM 1716 CZ ARG B 350 70.128 29.218 40.860 1.00 29.79 B ATOM 1717 NH1 ARG B 350 70.956 29.416 41.878 1.00 31.36 B ATOM 1718 NH2 ARG B 350 70.604 28.990 39.642 1.00 31.57 B ATOM 1719 C ARG B 350 64.094 31.124 44.651 1.00 20.94 B ATOM 1720 O ARG B 350 63.103 30.429 44.893 1.00 20.47 B ATOM 1721 N LEU B 351 64.672 31.909 45.549 1.00 18.79 B ATOM 1722 CA LEU B 351 64.157 32.026 46.890 1.00 17.44 B ATOM 1723 CB LEU B 351 64.895 33.143 47.624 1.00 14.47 B ATOM 1724 CG LEU B 351 66.358 32.799 47.897 1.00 14.78 B ATOM 1725 CD1 LEU B 351 66.992 33.900 48.730 1.00 17.09 B ATOM 1726 CD2 LEU B 351 66.466 31.467 48.619 1.00 12.98 B ATOM 1727 C LEU B 351 62.638 32.247 46.942 1.00 18.50 B ATOM 1728 O LEU B 351 61.958 31.715 47.826 1.00 17.10 B ATOM 1729 N ARG B 352 62.092 33.003 45.995 1.00 18.20 B ATOM 1730 CA ARG B 352 60.652 33.246 45.997 1.00 20.70 B ATOM 1731 CB ARG B 352 60.301 34.404 45.060 1.00 22.90 B ATOM 1732 CG ARG B 352 58.821 34.519 44.704 1.00 21.25 B ATOM 1733 CD ARG B 352 58.577 35.861 44.037 1.00 24.96 B ATOM 1734 NE ARG B 352 59.336 36.027 42.793 1.00 26.60 B ATOM 1735 CZ ARG B 352 58.840 35.772 41.588 1.00 24.08 B ATOM 1736 NH1 ARG B 352 57.589 35.344 41.468 1.00 25.95 B ATOM 1737 NH2 ARG B 352 59.582 35.955 40.508 1.00 23.94 B ATOM 1738 C ARG B 352 59.868 32.014 45.590 1.00 20.80 B ATOM 1739 O ARG B 352 58.812 31.701 46.151 1.00 20.69 B ATOM 1740 N LEU B 353 60.385 31.308 44.601 1.00 22.07 B ATOM 1741 CA LEU B 353 59.703 30.115 44.135 1.00 24.32 B ATOM 1742 CB LEU B 353 60.494 29.510 42.971 1.00 24.67 B ATOM 1743 CG LEU B 353 59.774 28.524 42.058 1.00 26.68 B ATOM 1744 CO1 LEU B 353 59.623 27.208 42.767 1.00 28.84 B ATOM 1745 CD2 LEU B 353 58.420 29.098 41.635 1.00 28.75 B ATOM 1746 C LEU B 353 59.614 29.166 45.336 1.00 25.14 B ATOM 1747 O LEU B 353 58.568 28.566 45.604 1.00 24.06 B ATOM 1748 N SER B 354 60.728 29.085 46.063 1.00 25.53 B ATOM 1749 CA SER B 354 60.867 28.264 47.262 1.00 26.14 B ATOM 1750 CB SER B 354 62.273 28.450 47.849 1.00 25.96 B ATOM 1751 OG SER B 354 62.454 27.730 49.061 1.00 23.97 B ATOM 1752 C SER B 354 59.830 28.656 48.313 1.00 27.19 B ATOM 1753 O SER B 354 59.098 27.818 48.837 1.00 27.24 B ATOM 1754 N PHE B 355 59.769 29.941 48.625 1.00 27.04 B ATOM 1755 CA PHE B 355 58.822 30.390 49.616 1.00 26.23 B ATOM 1756 CB PHE B 355 58.954 31.882 49.854 1.00 27.13 B ATOM 1757 CG PHE B 355 58.041 32.400 50.920 1.00 26.97 B ATOM 1758 CD1 PHE B 355 56.736 32.763 50.626 1.00 26.60 B ATOM 1759 CD2 PHE B 355 58.495 32.522 52.228 1.00 28.32 B ATOM 1760 CE1 PHE B 355 55.892 33.236 51.626 1.00 27.60 B ATOM 1761 CE2 PHE B 355 57.661 32.992 53.237 1.00 26.91 B ATOM 1762 CZ PHE B 355 56.360 33.353 52.934 1.00 27.81 B ATOM 1763 C PHE B 355 57.413 30.087 49.203 1.00 25.95 B ATOM 1764 O PHE B 355 56.687 29.427 49.929 1.00 25.86 B ATOM 1765 N LEU B 356 57.015 30.575 48.037 1.00 27.00 B ATOM 1766 CA LEU B 356 55.655 30.337 47.570 1.00 27.63 B ATOM 1767 CB LEU B 356 55.487 30.886 46.144 1.00 28.43 B ATOM 1768 CG LEU B 356 55.485 32.412 45.923 1.00 28.92 B ATOM 1769 CD1 LEU B 356 55.449 32.704 44.421 1.00 28.25 B ATOM 1770 CD2 LEU B 356 54.299 33.063 46.620 1.00 26.99 B ATOM 1771 C LEU B 356 55.297 28.842 47.618 1.00 26.51 B ATOM 1772 O LEU B 356 54.170 28.492 47.910 1.00 25.42 B ATOM 1773 N GLU B 357 56.267 27.976 47.343 1.00 27.82 B ATOM 1774 CA GLU B 357 56.051 26.537 47.357 1.00 28.89 B ATOM 1775 CB GLU B 357 57.223 25.841 46.668 1.00 30.18 B ATOM 1776 CG GLU B 357 57.193 24.319 46.727 1.00 34.82 B ATOM 1777 CD GLU B 357 58.032 23.659 45.640 1.00 38.48 B ATOM 1778 OE1 GLU B 357 59.254 23.926 45.569 1.00 41.06 B ATOM 1779 OE2 GLU B 357 57.460 22.870 44.849 1.00 40.28 B ATOM 1780 C GLU B 357 55.899 26.016 48.790 1.00 29.56 B ATOM 1781 O GLU B 357 55.055 25.165 49.072 1.00 30.56 B ATOM 1782 N ASN B 358 56.722 26.529 49.692 1.00 27.38 B ATOM 1783 CA ASN B 358 56.659 26.124 51.072 1.00 26.16 B ATOM 1784 CB ASN B 358 57.913 26.583 51.804 1.00 24.91 B ATOM 1785 CG ASN B 358 58.964 25.505 51.866 1.00 24.24 B ATOM 1786 OD1 ASN B 358 60.149 25.794 51.827 1.00 24.48 B ATOM 1787 ND2 ASN B 358 58.530 24.242 51.976 1.00 23.61 B ATOM 1788 C ASN B 358 55.440 26.669 51.796 1.00 27.01 B ATOM 1789 O ASN B 358 54.743 25.940 52.500 1.00 29.45 B ATOM 1790 N ILE B 359 55.169 27.948 51.603 1.00 25.54 B ATOM 1791 CA ILE B 359 54.066 28.576 52.287 1.00 24.86 B ATOM 1792 CB ILE B 359 53.989 30.111 51.964 1.00 23.57 B ATOM 1793 CG2 ILE B 359 53.438 30.361 50.544 1.00 22.38 B ATOM 1794 CG1 ILE B 359 53.099 30.808 52.994 1.00 21.88 B ATOM 1795 CD1 ILE B 359 53.627 30.735 54.428 1.00 17.84 B ATOM 1796 C ILE B 359 52.726 27.929 51.992 1.00 27.18 B ATOM 1797 O ILE B 359 51.864 27.842 52.859 1.00 27.37 B ATOM 1798 N PHE B 360 52.533 27.457 50.775 1.00 29.04 B ATOM 1799 CA PHE B 360 51.260 26.850 50.480 1.00 30.13 B ATOM 1800 CB PHE B 360 50.977 26.994 48.976 1.00 31.09 B ATOM 1801 CG PHE B 360 50.729 28.441 48.552 1.00 35.13 B ATOM 1802 CD1 PHE B 360 49.750 29.214 49.196 1.00 36.04 B ATOM 1803 CD2 PHE B 360 51.480 29.040 47.540 1.00 35.99 B ATOM 1804 CE1 PHE B 360 49.531 30.554 48.837 1.00 36.47 B ATOM 1805 CE2 PHE B 360 51.265 30.380 47.177 1.00 37.16 B ATOM 1806 CZ PHE B 360 50.290 31.138 47.827 1.00 35.98 B ATOM 1807 C PHE B 360 51.137 25.414 51.019 1.00 28.89 B ATOM 1808 O PHE B 360 50.040 24.932 51.282 1.00 29.91 B ATOM 1809 N ILE B 361 52.258 24.739 51.221 1.00 26.91 B ATOM 1810 CA ILE B 361 52.212 23.405 51.799 1.00 25.90 B ATOM 1811 CE ILE B 361 53.567 22.687 51.626 1.00 24.75 B ATOM 1812 CG2 ILE B 361 53.707 21.556 52.648 1.00 20.19 B ATOM 1813 CG1 ILE B 361 53.695 22.198 50.187 1.00 21.38 B ATOM 1814 CD1 ILE B 361 55.017 21.579 49.880 1.00 21.49 B ATOM 1815 C ILE B 361 51.894 23.539 53.303 1.00 25.76 B ATOM 1816 O ILE B 361 51.165 22.724 53.854 1.00 25.25 B ATOM 1817 N LEU B 362 52.455 24.558 53.955 1.00 24.78 B ATOM 1818 CA LEU B 362 52.200 24.780 55.367 1.00 24.80 B ATOM 1819 CB LEU B 362 53.097 25.890 55.942 1.00 24.95 B ATOM 1820 CG LEU B 362 52.861 26.232 57.439 1.00 25.61 B ATOM 1821 CD1 LEU B 362 53.251 25.034 58.290 1.00 23.05 B ATOM 1822 CD2 LEU B 362 53.682 27.448 57.891 1.00 24.66 B ATOM 1823 C LEU B 362 50.746 25.192 55.479 1.00 24.68 B ATOM 1824 O LEU B 362 50.075 24.847 56.440 1.00 25.14 B ATOM 1825 N LYS B 363 50.262 25.932 54.485 1.00 26.90 B ATOM 1826 CA LYS B 363 48.870 26.397 54.455 1.00 28.18 B ATOM 1827 CB LYS B 363 48.607 27.192 53.178 1.00 30.22 B ATOM 1828 CG LYS B 363 48.946 28.677 53.262 1.00 34.21 B ATOM 1829 CD LYS B 363 47.787 29.466 53.860 1.00 35.29 B ATOM 1830 CE LYS B 363 48.036 30.984 53.859 1.00 38.15 B ATOM 1831 NZ LYS B 363 48.196 31.608 52.486 1.00 38.16 B ATOM 1832 C LYS B 363 47.931 25.209 54.497 1.00 27.14 B ATOM 1833 O LYS B 363 46.852 25.288 55.076 1.00 27.91 B ATOM 1834 N ASN B 364 48.365 24.119 53.872 1.00 26.50 B ATOM 1835 CA ASN B 364 47.602 22.893 53.809 1.00 28.02 B ATOM 1836 CB ASN B 364 48.119 21.990 52.692 1.00 29.30 B ATOM 1837 CG ASN B 364 47.742 22.485 51.311 1.00 30.37 B ATOM 1838 OD1 ASN B 364 48.127 21.882 50.299 1.00 29.53 B ATOM 1839 ND2 ASN B 364 46.982 23.584 51.255 1.00 31.60 B ATOM 1840 C ASN B 364 47.696 22.129 55.106 1.00 27.69 B ATOM 1841 O ASN B 364 46.716 21.551 55.559 1.00 28.47 B ATOM 1842 N TRP B 365 48.882 22.093 55.693 1.00 26.51 B ATOM 1843 CA TRP B 365 49.039 21.371 56.938 1.00 27.73 B ATOM 1844 CB TRP B 365 50.489 21.397 57.400 1.00 29.20 B ATOM 1845 CG TRP B 365 51.351 20.381 56.790 1.00 29.13 B ATOM 1846 CD2 TRP B 365 51.742 19.142 57.379 1.00 29.19 B ATOM 1847 CE2 TRP B 365 52.638 18.523 56.489 1.00 28.54 B ATOM 1848 CE3 TRP B 365 51.425 18.495 58.579 1.00 29.88 B ATOM 1849 CD1 TRP B 365 51.989 20.460 55.598 1.00 28.45 B ATOM 1850 NE1 TRP B 365 52.771 19.351 55.406 1.00 27.81 B ATOM 1851 CZ2 TRP B 365 53.230 17.282 56.758 1.00 28.80 B ATOM 1852 CZ3 TRP B 365 52.018 17.257 58.842 1.00 29.52 B ATOM 1853 CH2 TRP B 365 52.909 16.671 57.934 1.00 27.59 B ATOM 1854 C TRP B 365 48.183 21.976 58.037 1.00 27.25 B ATOM 1855 O TRP B 365 47.686 21.262 58.898 1.00 27.54 B ATOM 1856 N TYR B 366 48.015 23.293 57.985 1.00 25.59 B ATOM 1857 CA TYR B 366 47.271 24.038 58.989 1.00 25.83 B ATOM 1858 CB TYR B 366 47.858 25.433 59.127 1.00 24.61 B ATOM 1859 CG TYR B 366 49.220 25.559 59.761 1.00 22.97 B ATOM 1860 CD1 TYR B 366 49.803 24.511 60.469 1.00 23.61 B ATOM 1861 CE1 TYR B 366 50.999 24.699 61.170 1.00 21.04 B ATOM 1862 CD2 TYR B 366 49.871 26.779 59.760 1.00 21.89 B ATOM 1863 CE2 TYR B 366 51.050 26.968 60.452 1.00 20.89 B ATOM 1864 CZ TYR B 366 51.603 25.940 61.153 1.00 20.92 B ATOM 1865 OH TYR B 366 52.741 26.179 61.878 1.00 21.34 B ATOM 1866 C TYR B 366 45.781 24.205 58.730 1.00 26.75 B ATOM 1867 O TYR B 366 45.053 24.659 59.618 1.00 25.47 B ATOM 1868 N ASN B 367 45.343 23.874 57.516 1.00 27.78 B ATOM 1869 CA ASN B 367 43.935 23.993 57.137 1.00 28.96 B ATOM 1870 CB ASN B 367 43.789 24.062 55.611 1.00 27.81 B ATOM 1871 CG ASN B 367 42.420 24.542 55.172 1.00 27.70 B ATOM 1872 OD1 ASN B 367 41.462 24.533 55.944 1.00 29.38 B ATOM 1873 ND2 ASN B 367 42.321 24.957 53.915 1.00 27.06 B ATOM 1874 C ASN B 367 43.184 22.772 57.668 1.00 29.83 B ATOM 1875 O ASN B 367 43.454 21.638 57.253 1.00 30.52 B ATOM 1876 N PRO B 368 42.246 22.988 58.613 1.00 30.10 B ATOM 1877 CD PRO B 368 41.884 24.278 59.227 1.00 28.86 B ATOM 1878 CA PRO B 368 41.458 21.889 59.200 1.00 29.62 B ATOM 1879 CB PRO B 368 40.654 22.578 60.304 1.00 28.09 B ATOM 1880 CG PRO B 368 41.398 23.839 60.573 1.00 28.33 B ATOM 1881 C PRO B 368 40.534 21.318 58.133 1.00 29.34 B ATOM 1882 O PRO B 368 40.223 20.133 58.118 1.00 28.44 B ATOM 1883 N LYS B 369 40.083 22.202 57.256 1.00 29.08 B ATOM 1884 CA LYS B 369 39.202 21.814 56.187 1.00 30.72 B ATOM 1885 CB LYS B 369 38.417 23.044 55.697 1.00 32.78 B ATOM 1886 CG LYS B 369 37.095 23.310 56.487 1.00 34.07 B ATOM 1887 CD LYS B 369 36.649 24.778 56.462 1.00 36.76 B ATOM 1888 CE LYS B 369 36.882 25.442 55.098 1.00 38.43 B ATOM 1889 NZ LYS B 369 36.568 26.906 55.151 1.00 41.21 B ATOM 1890 C LYS B 369 39.977 21.145 55.050 1.00 30.60 B ATOM 1891 O LYS B 369 39.389 20.779 54.040 1.00 32.44 B ATOM 1892 N PHE B 370 41.293 20.985 55.207 1.00 29.96 B ATOM 1893 CA PHE B 370 42.111 20.335 54.175 1.00 28.15 B ATOM 1894 CB PHE B 370 43.422 21.107 53.934 1.00 29.31 B ATOM 1895 CG PHE B 370 44.447 20.330 53.124 1.00 31.81 B ATOM 1896 CD1 PHE B 370 45.283 19.394 53.738 1.00 34.71 B ATOM 1897 CD2 PHE B 370 44.536 20.484 51.745 1.00 31.92 B ATOM 1898 CE1 PHE B 370 46.185 18.625 52.992 1.00 34.80 B ATOM 1899 CE2 PHE B 370 45.436 19.718 50.992 1.00 33.21 B ATOM 1900 CZ PHE B 370 46.259 18.785 51.622 1.00 33.35 B ATOM 1901 C PHE B 370 42.431 18.886 54.537 1.00 26.13 B ATOM 1902 O PHE B 370 42.750 18.584 55.682 1.00 26.19 B ATOM 1903 N VAL B 371 42.352 17.993 53.556 1.00 25.26 B ATOM 1904 CA VAL B 371 42.656 16.590 53.811 1.00 24.76 B ATOM 1905 CB VAL B 371 41.419 15.694 53.697 1.00 25.22 B ATOM 1906 CG1 VAL B 371 41.736 14.297 54.237 1.00 22.91 B ATOM 1907 CG2 VAL B 371 40.257 16.324 54.442 1.00 23.49 B ATOM 1908 C VAL B 371 43.712 16.062 52.863 1.00 24.14 B ATOM 1909 O VAL B 371 43.585 16.188 51.653 1.00 23.89 B ATOM 1910 N PRO B 372 44.767 15.447 53.418 1.00 24.76 B ATOM 1911 CD PRO B 372 44.861 15.087 54.840 1.00 25.65 B ATOM 1912 CA PRO B 372 45.889 14.878 52.678 1.00 25.57 B ATOM 1913 CB PRO B 372 46.835 14.390 53.769 1.00 25.32 B ATOM 1914 CG PRO B 372 46.318 14.998 55.041 1.00 26.54 B ATOM 1915 C PRO B 372 45.421 13.720 51.863 1.00 27.92 B ATOM 1916 O PRO B 372 44.359 13.144 52.143 1.00 29.78 B ATOM 1917 N GLN B 373 46.223 13.375 50.858 1.00 28.98 B ATOM 1918 CA GLN B 373 45.940 12.222 50.002 1.00 29.41 B ATOM 1919 CB GLN B 373 46.566 12.412 48.600 1.00 29.51 B ATOM 1920 CG GLN B 373 45.660 13.145 47.586 1.00 29.73 B ATOM 1921 CD GLN B 373 46.354 13.455 46.247 1.00 30.26 B ATOM 1922 OE1 GLN B 373 47.091 14.429 46.129 1.00 30.70 B ATOM 1923 NE2 GLN B 373 46.113 12.621 45.240 1.00 30.61 B ATOM 1924 C GLN B 373 46.554 11.029 50.758 1.00 28.67 B ATOM 1925 O GLN B 373 47.662 11.119 51.274 1.00 28.24 B ATOM 1926 N ARG B 374 45.803 9.936 50.845 1.00 28.06 B ATOM 1927 CA ARG B 374 46.213 8.728 51.557 1.00 25.68 B ATOM 1928 CB ARG B 374 45.030 8.254 52.416 1.00 25.68 B ATOM 1929 CG ARG B 374 45.173 6.929 53.159 1.00 24.87 B ATOM 1930 CD ARG B 374 45.727 7.099 54.544 1.00 25.14 B ATOM 1931 NE ARG B 374 45.604 5.872 55.347 1.00 26.59 B ATOM 1932 CZ ARG B 374 44.549 5.554 56.099 1.00 24.91 B ATOM 1933 NH1 ARG B 374 43.503 6.370 56.171 1.00 23.91 B ATOM 1934 NH2 ARG B 374 44.533 4.407 56.770 1.00 23.39 B ATOM 1935 C ARG B 374 46.650 7.619 50.598 1.00 25.60 B ATOM 1936 O ARG B 374 45.978 7.352 49.591 1.00 25.61 B ATOM 1937 N THR B 375 47.790 7.000 50.909 1.00 24.83 B ATOM 1938 CA THR B 375 48.325 5.895 50.124 1.00 24.29 B ATOM 1939 CB THR B 375 49.562 6.298 49.278 1.00 24.62 B ATOM 1940 OG1 THR B 375 49.334 7.559 48.630 1.00 26.27 B ATOM 1941 CG2 THR B 375 49.845 5.228 48.217 1.00 22.20 B ATOM 1942 C THR B 375 48.787 4.844 51.125 1.00 25.05 B ATOM 1943 O THR B 375 49.710 5.108 51.889 1.00 25.56 B ATOM 1944 N THR B 376 48.149 3.669 51.122 1.00 25.33 B ATOM 1945 CA THR B 376 48.509 2.571 52.034 1.00 25.61 B ATOM 1946 CB THR B 376 47.254 1.951 52.733 1.00 23.00 B ATOM 1947 OG1 THR B 376 46.361 2.992 53.148 1.00 23.90 B ATOM 1948 CG2 THR B 376 47.678 1.125 53.956 1.00 21.63 B ATOM 1949 C THR B 376 49.224 1.439 51.273 1.00 27.50 B ATOM 1950 O THR B 376 48.696 0.916 50.303 1.00 27.69 B ATOM 1951 N LEU B 377 50.413 1.058 51.735 1.00 29.38 B ATOM 1952 CA LEU B 377 51.204 −0.001 51.119 1.00 29.82 B ATOM 1953 CB LEU B 377 52.540 0.574 50.650 1.00 27.89 B ATOM 1954 CG LEU B 377 52.396 1.871 49.837 1.00 27.64 B ATOM 1955 CD1 LEU B 377 53.754 2.507 49.549 1.00 23.10 B ATOM 1956 CD2 LEU B 377 51.643 1.570 48.562 1.00 26.07 B ATOM 1957 C LEU B 377 51.451 −1.131 52.125 1.00 32.73 B ATOM 1958 O LEU B 377 51.328 −0.925 53.327 1.00 32.89 B ATOM 1959 N ARG B 378 51.815 −2.315 51.633 1.00 36.51 B ATOM 1960 CA ARG B 378 52.071 −3.463 52.498 1.00 39.20 B ATOM 1961 CB ARG B 378 52.180 −4.757 51.678 1.00 42.06 B ATOM 1962 CG ARG B 378 52.510 −6.019 52.506 1.00 45.42 B ATOM 1963 CD ARG B 378 52.472 −7.335 51.682 1.00 48.17 B ATOM 1964 NE ARG B 378 51.210 −7.513 50.958 1.00 51.30 B ATOM 1965 CZ ARG B 378 50.850 −8.616 50.306 1.00 52.70 B ATOM 1966 NH1 ARG B 378 51.655 −9.673 50.281 1.00 53.25 B ATOM 1967 NH2 ARG B 378 49.684 −8.654 49.664 1.00 54.26 B ATOM 1968 C ARG B 378 53.333 −3.278 53.307 1.00 40.74 B ATOM 1969 O ARG B 378 54.339 −2.747 52.819 1.00 40.15 B ATOM 1970 N GLY B 379 53.266 −3.735 54.555 1.00 42.99 B ATOM 1971 CA GLY B 379 54.394 −3.628 55.463 1.00 43.31 B ATOM 1972 C GLY B 379 55.221 −4.897 55.532 1.00 43.80 B ATOM 1973 O GLY B 379 55.501 −5.532 54.516 1.00 42.41 B ATOM 1974 N HIS B 380 55.609 −5.264 56.747 1.00 44.62 B ATOM 1975 CA HIS B 380 56.421 −6.451 56.972 1.00 45.57 B ATOM 1976 CB HIS B 380 57.468 −6.163 58.049 1.00 42.95 B ATOM 1977 CG HIS B 380 58.489 −5.148 57.640 1.00 41.43 B ATOM 1978 CD2 HIS B 380 58.369 −3.842 57.307 1.00 39.61 B ATOM 1979 ND1 HIS B 380 59.833 −5.444 57.559 1.00 40.42 B ATOM 1980 CE1 HIS B 380 60.497 −4.362 57.195 1.00 39.52 B ATOM 1981 NE2 HIS B 380 59.633 −3.376 57.037 1.00 39.67 B ATOM 1982 C HIS B 380 55.552 −7.627 57.398 1.00 47.13 B ATOM 1983 O HIS B 380 54.374 −7.457 57.690 1.00 47.01 B ATOM 1984 N MSE B 381 56.127 −8.822 57.440 1.00 49.63 B ATOM 1985 CA MSE B 381 55.350 −9.979 57.826 1.00 51.34 B ATOM 1986 CB MSE B 381 56.181 −11.238 57.658 1.00 54.42 B ATOM 1987 CG MSE B 381 56.131 −11.740 56.225 1.00 60.08 B ATOM 1988 SE MSE B 381 57.583 −12.923 55.737 1.00 69.56 B ATOM 1989 CE MSE B 381 56.901 −14.517 56.629 1.00 64.33 B ATOM 1990 C MSE B 381 54.800 −9.860 59.227 1.00 51.47 B ATOM 1991 O MSE B 381 53.645 −10.193 59.464 1.00 53.52 B ATOM 1992 N THR B 382 55.608 −9.366 60.158 1.00 50.41 B ATOM 1993 CA THR B 382 55.159 −9.204 61.539 1.00 48.29 B ATOM 1994 CB THR B 382 56.367 −9.222 62.513 1.00 48.92 B ATOM 1995 OG1 THR B 382 55.931 −8.858 63.825 1.00 49.73 B ATOM 1996 CG2 THR B 382 57.457 −8.259 62.048 1.00 51.19 B ATOM 1997 C THR B 382 54.361 −7.903 61.674 1.00 46.73 B ATOM 1998 O THR B 382 54.511 −6.990 60.858 1.00 45.72 B ATOM 1999 N SER B 383 53.510 −7.818 62.695 1.00 45.75 B ATOM 2000 CA SER B 383 52.667 −6.631 62.888 1.00 44.00 B ATOM 2001 CB SER B 383 51.418 −6.988 63.706 1.00 44.17 B ATOM 2002 OG SER B 383 51.707 −6.998 65.093 1.00 44.67 B ATOM 2003 C SER B 383 53.363 −5.440 63.552 1.00 42.52 B ATOM 2004 O SER B 383 52.739 −4.400 63.769 1.00 42.16 B ATOM 2005 N VAL B 384 54.645 −5.584 63.875 1.00 40.61 B ATOM 2006 CA VAL B 384 55.368 −4.496 64.519 1.00 38.88 B ATOM 2007 CB VAL B 384 55.785 −4.868 65.971 1.00 37.56 B ATOM 2008 CG1 VAL B 384 56.490 −3.706 66.635 1.00 34.97 B ATOM 2009 CG2 VAL B 384 54.570 −5.273 66.772 1.00 37.83 B ATOM 2010 C VAL B 384 56.617 −4.090 63.756 1.00 38.38 B ATOM 2011 O VAL B 384 57.507 −4.906 63.506 1.00 38.18 B ATOM 2012 N ILE B 385 56.674 −2.823 63.372 1.00 37.92 B ATOM 2013 CA ILE B 385 57.842 −2.330 62.674 1.00 38.47 B ATOM 2014 CB ILE B 385 57.462 −1.284 61.570 1.00 38.37 B ATOM 2015 CG2 ILE B 385 58.692 −0.795 60.853 1.00 35.43 B ATOM 2016 CG1 ILE B 385 56.610 −1.951 60.483 1.00 38.29 B ATOM 2017 CD1 ILE B 385 56.296 −1.048 59.293 1.00 40.13 B ATOM 2018 C ILE B 385 58.752 −1.744 63.758 1.00 38.62 B ATOM 2019 O ILE B 385 58.295 −1.054 64.679 1.00 39.76 B ATOM 2020 N THR B 386 60.040 −2.057 63.649 1.00 37.77 B ATOM 2021 CA THR B 386 61.053 −1.643 64.616 1.00 34.37 B ATOM 2022 CB THP. B 386 62.142 −2.722 64.734 1.00 32.81 B ATOM 2023 OG1 THR B 386 62.810 −2.855 63.473 1.00 31.89 B ATOM 2024 CG2 THR B 386 61.528 −4.050 65.098 1.00 32.45 B ATOM 2025 C THR B 386 61.740 −0.329 64.281 1.00 32.70 B ATOM 2026 O THR B 386 62.088 0.438 65.167 1.00 33.06 B ATOM 2027 N CYS B 387 61.947 −0.058 63.005 1.00 31.07 B ATOM 2028 CA CYS B 387 62.627 1.178 62.659 1.00 30.70 B ATOM 2029 CB CYS B 387 64.140 0.964 62.769 1.00 29.49 B ATOM 2030 SG CYS B 387 64.707 −0.568 62.008 1.00 32.59 B ATOM 2031 C CYS B 387 62.250 1.702 61.268 1.00 29.94 B ATOM 2032 O CYS B 387 61.896 0.927 60.365 1.00 27.25 B ATOM 2033 N LEU B 388 62.349 3.021 61.097 1.00 29.32 B ATOM 2034 CA LEU B 388 62.001 3.659 59.828 1.00 28.34 B ATOM 2035 CB LEU B 388 60.534 4.097 59.878 1.00 28.15 B ATOM 2036 CG LEU B 388 59.848 4.716 58.662 1.00 25.84 B ATOM 2037 CD1 LEU B 388 58.358 4.729 58.925 1.00 26.04 B ATOM 2038 CD2 LEU B 388 60.361 6.117 58.401 1.00 24.86 B ATOM 2039 C LEU B 388 62.885 4.851 59.479 1.00 26.75 B ATOM 2040 O LEU B 388 63.211 5.661 60.336 1.00 25.66 B ATOM 2041 N GLN B 389 63.284 4.947 58.214 1.00 27.43 B ATOM 2042 CA GLN B 389 64.112 6.067 57.753 1.00 27.85 B ATOM 2043 CB GLN B 389 65.505 5.589 57.308 1.00 28.80 B ATOM 2044 CG GLN B 389 66.450 5.215 58.443 1.00 29.07 B ATOM 2045 CD GLN B 389 66.900 6.425 59.249 1.00 29.82 B ATOM 2046 OE1 GLN B 389 67.815 7.152 58.849 1.00 30.35 B ATOM 2047 NE2 GLN B 389 66.244 6.654 60.383 1.00 27.50 B ATOM 2048 C GLN B 389 63.417 6.718 56.577 1.00 26.75 B ATOM 2049 O GLN B 389 62.792 6.035 55.766 1.00 26.92 B ATOM 2050 N PHE B 390 63.532 8.037 56.483 1.00 26.42 B ATOM 2051 CA PHE B 390 62.928 8.778 55.382 1.00 26.53 B ATOM 2052 CB PHE B 390 61.606 9.405 55.833 1.00 24.52 B ATOM 2053 CG PHE B 390 60.846 10.069 54.728 1.00 23.83 B ATOM 2054 CD1 PHE B 390 60.614 9.408 53.530 1.00 24.31 B ATOM 2055 CD2 PHE B 390 60.357 11.358 54.883 1.00 24.82 B ATOM 2056 CE1 PHE B 390 59.906 10.021 52.496 1.00 24.43 B ATOM 2057 CE2 PHE B 390 59.643 11.985 53.851 1.00 26.18 B ATOM 2058 CZ PHE B 390 59.418 11.316 52.657 1.00 25.05 B ATOM 2059 C PHE B 390 63.885 9.852 54.853 1.00 28.00 B ATOM 2060 O PHE B 390 64.003 10.930 55.439 1.00 26.52 B ATOM 2061 N GLU B 391 64.591 9.532 53.761 1.00 31.44 B ATOM 2062 CA GLU B 391 65.552 10.459 53.112 1.00 34.19 B ATOM 2063 CB GLU B 391 66.958 10.374 53.753 1.00 35.50 B ATOM 2064 CG GLU B 391 67.082 9.731 55.143 1.00 38.57 B ATOM 2065 CD GLU B 391 66.652 10.654 56.306 1.00 40.82 B ATOM 2066 OE1 GLU B 391 66.842 11.896 56.199 1.00 38.26 B ATOM 2067 OE2 GLU B 391 66.138 10.116 57.327 1.00 41.64 B ATOM 2068 C GLU B 391 65.706 10.165 51.602 1.00 34.30 B ATOM 2069 O GLU B 391 65.415 9.060 51.141 1.00 32.53 B ATOM 2070 N ASP B 392 66.179 11.151 50.842 1.00 35.27 B ATOM 2071 CA ASP B 392 66.388 10.979 49.395 1.00 35.87 B ATOM 2072 CB ASP B 392 67.633 10.114 49.106 1.00 35.92 B ATOM 2073 CG ASP B 392 68.941 10.886 49.139 1.00 36.64 B ATOM 2074 OD1 ASP B 392 68.967 12.093 48.795 1.00 37.84 B ATOM 2075 OD2 ASP B 392 69.964 10.253 49.492 1.00 36.21 B ATOM 2076 C ASP B 392 65.215 10.300 48.673 1.00 36.11 B ATOM 2077 O ASP B 392 65.452 9.465 47.805 1.00 36.71 B ATOM 2078 N ASN B 393 63.968 10.618 49.018 1.00 35.71 B ATOM 2079 CA ASN B 393 62.805 9.999 48.347 1.00 35.51 B ATOM 2080 CB ASN B 393 62.861 10.281 46.847 1.00 34.88 B ATOM 2081 CG ASN B 393 62.762 11.755 46.544 1.00 37.09 B ATOM 2082 OD1 ASN B 393 61.672 12.328 46.584 1.00 36.85 B ATOM 2083 ND2 ASN B 393 63.903 12.388 46.255 1.00 37.57 B ATOM 2084 C ASN B 393 62.633 8.489 48.570 1.00 35.26 B ATOM 2085 O ASN B 393 61.925 7.805 47.817 1.00 34.05 B ATOM 2086 N TYR B 394 63.283 7.990 49.618 1.00 35.44 B ATOM 2087 CA TYR B 394 63.246 6.585 50.004 1.00 33.92 B ATOM 2088 CB TYR B 394 64.660 6.006 50.087 1.00 34.53 B ATOM 2089 CG TYR B 394 65.314 5.705 48.772 1.00 35.08 B ATOM 2090 CD1 TYR B 394 64.808 4.707 47.944 1.00 33.82 B ATOM 2091 CE1 TYR B 394 65.424 4.394 46.753 1.00 35.67 B ATOM 2092 CD2 TYR B 394 66.461 6.393 48.370 1.00 33.92 B ATOM 2093 CE2 TYR B 394 67.093 6.091 47.179 1.00 36.23 B ATOM 2094 CZ TYR B 394 66.571 5.090 46.369 1.00 37.49 B ATOM 2095 OH TYR B 394 67.184 4.785 45.167 1.00 39.46 B ATOM 2096 C TYR B 394 62.652 6.473 51.393 1.00 33.94 B ATOM 2097 O TYR B 394 62.973 7.268 52.281 1.00 32.72 B ATOM 2098 N VAL B 395 61.804 5.470 51.575 1.00 33.59 B ATOM 2099 CA VAL B 395 61.200 5.196 52.864 1.00 33.27 B ATOM 2100 CB VAL B 395 59.655 5.170 52.787 1.00 33.84 B ATOM 2101 CG1 VAL B 395 59.055 4.927 54.167 1.00 32.25 B ATOM 2102 CG2 VAL B 395 59.145 6.467 52.213 1.00 34.69 B ATOM 2103 C VAL B 395 61.708 3.803 53.182 1.00 33.68 B ATOM 2104 O VAL B 395 61.334 2.822 52.526 1.00 35.51 B ATOM 2105 N ILE B 396 62.592 3.701 54.163 1.00 33.52 B ATOM 2106 CA ILE B 396 63.113 2.386 54.508 1.00 32.85 B ATOM 2107 CB ILE B 396 64.666 2.403 54.579 1.00 33.18 B ATOM 2108 CG2 ILE B 396 65.207 0.998 54.438 1.00 32.95 B ATOM 2109 CG1 ILE B 396 65.238 3.231 53.434 1.00 32.57 B ATOM 2110 CD1 ILE B 396 66.704 3.519 53.594 1.00 34.98 B ATOM 2111 C ILE B 396 62.527 1.999 55.862 1.00 30.96 B ATOM 2112 O ILE B 396 62.550 2.787 56.805 1.00 29.47 B ATOM 2113 N THR B 397 61.977 0.792 55.943 1.00 29.81 B ATOM 2114 CA THR B 397 61.397 0.303 57.188 1.00 30.52 B ATOM 2115 CB THR B 397 59.883 0.014 57.087 1.00 28.68 B ATOM 2116 OG1 THR B 397 59.685 −1.096 56.216 1.00 27.52 B ATOM 2117 CG2 THR B 397 59.127 1.206 56.561 1.00 28.88 B ATOM 2118 C THR B 397 62.052 −1.012 57.574 1.00 32.66 B ATOM 2119 O THR B 397 62.495 −1.768 56.708 1.00 32.93 B ATOM 2120 N GLY B 398 62.095 −1.283 58.878 1.00 34.04 B ATOM 2121 CA GLY B 398 62.673 −2.521 59.377 1.00 36.31 B ATOM 2122 C GLY B 398 61.790 −3.205 60.409 1.00 38.57 B ATOM 2123 O GLY B 398 61.203 −2.535 61.257 1.00 38.84 B ATOM 2124 N ALA B 399 61.692 −4.532 60.347 1.00 40.48 B ATOM 2125 CA ALA B 399 60.870 −5.274 61.304 1.00 43.09 B ATOM 2126 CB ALA B 399 59.540 −5.687 60.660 1.00 43.54 B ATOM 2127 C ALA B 399 61.577 −6.506 61.870 1.00 44.04 B ATOM 2128 O ALA B 399 62.688 −6.838 61.461 1.00 43.75 B ATOM 2129 N ASP B 400 60.921 −7.182 62.811 1.00 45.72 B ATOM 2130 CA ASP B 400 61.498 −8.363 63.446 1.00 47.39 B ATOM 2131 CB ASP B 400 60.854 −8.596 64.820 1.00 48.07 B ATOM 2132 CG ASP B 400 61.569 −9.666 65.626 1.00 48.91 B ATOM 2133 OD1 ASP B 400 62.791 −9.515 65.869 1.00 49.38 B ATOM 2134 OD2 ASP B 400 60.910 −10.656 66.012 1.00 48.62 B ATOM 2135 C ASP B 400 61.347 −9.610 62.579 1.00 47.48 B ATOM 2136 O ASP B 400 61.522 −10.735 63.048 1.00 49.06 B ATOM 2137 N ASP B 401 61.014 −9.403 61.313 1.00 46.02 B ATOM 2138 CA ASP B 401 60.851 −10.501 60.378 1.00 43.80 B ATOM 2139 CB ASP B 401 59.688 −10.192 59.436 1.00 45.11 B ATOM 2140 CG ASP B 401 59.962 −8.996 58.541 1.00 46.35 B ATOM 2141 OD1 ASP B 401 60.797 −8.130 58.909 1.00 46.25 B ATOM 2142 OD2 ASP B 401 59.325 −8.919 57.465 1.00 47.47 B ATOM 2143 C ASP B 401 62.147 −10.661 59.592 1.00 42.18 B ATOM 2144 O ASP B 401 62.153 −11.209 58.498 1.00 40.84 B ATOM 2145 N LYS B 402 63.241 −10.171 60.174 1.00 42.03 B ATOM 2146 CA LYS B 402 64.581 −10.221 59.577 1.00 41.37 B ATOM 2147 CB LYS B 402 65.061 −11.671 59.394 1.00 41.89 B ATOM 2148 CG LYS B 402 64.777 −12.595 60.546 1.00 40.16 B ATOM 2149 CD LYS B 402 65.248 −14.004 60.249 1.00 39.21 B ATOM 2150 CE LYS B 402 64.973 −14.910 61.453 1.00 41.18 B ATOM 2151 NZ LYS B 402 65.506 −16.306 61.313 1.00 41.31 B ATOM 2152 C LYS B 402 64.584 −9.545 58.217 1.00 41.18 B ATOM 2153 O LYS B 402 65.387 −9.880 57.350 1.00 41.03 B ATOM 2154 N MSE B 403 63.700 −8.583 58.021 1.00 41.52 B ATOM 2155 CA MSE B 403 63.643 −7.932 56.731 1.00 41.52 B ATOM 2156 CB MSE B 403 62.364 −8.354 56.024 1.00 44.20 B ATOM 2157 CG MSE B 403 62.593 −8.927 54.649 1.00 49.51 B ATOM 2158 CE MSE B 403 63.401 −10.704 54.630 1.00 56.96 B ATOM 2159 CE MSE B 403 61.754 −11.724 54.910 1.00 52.63 B ATOM 2160 C MSE B 403 63.728 −6.408 56.765 1.00 39.82 B ATOM 2161 O MSE B 403 63.396 −5.758 57.763 1.00 39.40 B ATOM 2162 N ILE B 404 64.163 −5.861 55.638 1.00 37.19 B ATOM 2163 CA ILE B 404 64.305 −4.432 55.441 1.00 34.55 B ATOM 2164 CB ILE B 404 65.790 −4.049 55.290 1.00 33.79 B ATOM 2165 CG2 ILE B 404 65.904 −2.619 54.750 1.00 32.01 B ATOM 2166 CG1 ILE B 404 66.516 −4.256 56.628 1.00 32.98 B ATOM 2167 CD1 ILE B 404 68.003 −3.868 56.634 1.00 32.54 B ATOM 2168 C ILE B 404 63.576 −4.060 54.152 1.00 34.51 B ATOM 2169 O ILE B 404 63.994 −4.455 53.061 1.00 33.17 B ATOM 2170 N ARG B 405 62.489 −3.303 54.275 1.00 34.07 B ATOM 2171 CA ARG B 405 61.714 −2.890 53.104 1.00 34.11 B ATOM 2172 CB ARG B 405 60.222 −3.145 53.349 1.00 31.76 B ATOM 2173 CG ARG B 405 59.877 −4.612 53.569 1.00 29.64 B ATOM 2174 CD ARG B 405 58.419 −4.820 53.979 1.00 28.14 B ATOM 2175 NE ARG B 405 57.449 −4.457 52.948 1.00 28.57 B ATOM 2176 CZ ARG B 405 57.252 −5.129 51.813 1.00 28.90 B ATOM 2177 NH1 ARG B 405 57.964 −6.215 51.537 1.00 25.04 B ATOM 2178 NH2 ARG B 405 56.311 −4.728 50.960 1.00 29.02 B ATOM 2179 C ARG B 405 61.912 −1.425 52.730 1.00 34.97 B ATOM 2180 O ARG B 405 61.823 −0.545 53.580 1.00 37.29 B ATOM 2181 N VAL B 406 62.180 −1.157 51.460 1.00 34.65 B ATOM 2182 CA VAL B 406 62.353 0.218 51.027 1.00 35.39 B ATOM 2183 CB VAL B 406 63.710 0.421 50.341 1.00 38.27 B ATOM 2184 CG1 VAL B 406 63.886 −0.606 49.251 1.00 39.50 B ATOM 2185 CG2 VAL B 406 63.789 1.831 49.759 1.00 38.99 B ATOM 2186 C VAL B 406 61.257 0.576 50.041 1.00 34.13 B ATOM 2187 O VAL B 406 60.867 −0.250 49.213 1.00 35.33 B ATOM 2188 N TYR B 407 60.763 1.806 50.127 1.00 32.42 B ATOM 2189 CA TYR B 407 59.694 2.263 49.236 1.00 30.87 B ATOM 2190 CB TYR B 407 58.409 2.537 50.032 1.00 30.46 B ATOM 2191 CG TYR B 407 57.953 1.435 50.967 1.00 29.77 B ATOM 2192 CD1 TYR B 407 58.682 1.115 52.121 1.00 27.81 B ATOM 2193 CE1 TYR B 407 58.269 0.081 52.962 1.00 27.20 B ATOM 2194 CD2 TYR B 407 56.795 0.695 50.682 1.00 29.18 B ATOM 2195 CE2 TYR B 407 56.376 −0.335 51.511 1.00 27.89 B ATOM 2196 CZ TYR B 407 57.114 −0.645 52.646 1.00 27.80 B ATOM 2197 OH TYR B 407 56.711 −1.705 53.430 1.00 26.41 B ATOM 2198 C TYR B 407 60.058 3.552 48.507 1.00 29.93 B ATOM 2199 O TYR B 407 61.078 4.180 48.790 1.00 30.68 B ATOM 2200 N ASP B 408 59.189 3.947 47.583 1.00 29.96 B ATOM 2201 CA ASP B 408 59.360 5.181 46.825 1.00 30.52 B ATOM 2202 CB ASP B 408 59.226 4.920 45.325 1.00 32.17 B ATOM 2203 CG ASP B 408 59.430 6.178 44.504 1.00 35.42 B ATOM 2204 OD1 ASP B 408 60.450 6.868 44.721 1.00 37.74 B ATOM 2205 OD2 ASP B 408 58.579 6.483 43.644 1.00 37.68 B ATOM 2206 C ASP B 408 58.296 6.195 47.264 1.00 29.92 B ATOM 2207 O ASP B 408 57.095 5.995 47.024 1.00 29.81 B ATOM 2208 N SER B 409 58.743 7.284 47.895 1.00 28.80 B ATOM 2209 CA SER B 409 57.848 8.338 48.400 1.00 28.18 B ATOM 2210 CB SER B 409 58.581 9.202 49.442 1.00 25.85 B ATOM 2211 OG SER B 409 59.652 9.932 48.869 1.00 23.45 B ATOM 2212 C SER B 409 57.253 9.245 47.320 1.00 29.34 B ATOM 2213 O SER B 409 56.259 9.941 47.562 1.00 27.47 B ATOM 2214 N ILE B 410 57.861 9.224 46.133 1.00 31.65 B ATOM 2215 CA ILE B 410 57.421 10.037 44.994 1.00 34.03 B ATOM 2216 CB ILE B 410 58.558 10.242 43.972 1.00 35.56 B ATOM 2217 CG2 ILE B 410 58.032 11.052 42.783 1.00 34.67 B ATOM 2218 CG1 ILE B 410 59.747 10.947 44.616 1.00 34.10 B ATOM 2219 CD1 ILE B 410 60.988 10.910 43.752 1.00 33.88 B ATOM 2220 C ILE B 410 56.259 9.409 44.217 1.00 34.05 B ATOM 2221 O ILE B 410 55.330 10.101 43.818 1.00 33.24 B ATOM 2222 N ASN B 411 56.354 8.107 43.972 1.00 34.44 B ATOM 2223 CA ASN B 411 55.327 7.390 43.246 1.00 36.84 B ATOM 2224 CB ASN B 411 55.955 6.377 42.273 1.00 39.14 B ATOM 2225 CG ASN B 411 56.312 6.993 40.911 1.00 41.27 B ATOM 2226 OD1 ASN B 411 56.852 8.100 40.834 1.00 41.10 B ATOM 2227 ND2 ASN B 411 56.017 6.261 39.832 1.00 42.48 B ATOM 2228 C ASN B 411 54.428 6.663 44.238 1.00 37.14 B ATOM 2229 O ASN B 411 53.466 6.001 43.848 1.00 37.86 B ATOM 2230 N LYS B 412 54.748 6.776 45.522 1.00 36.65 B ATOM 2231 CA LYS B 412 53.944 6.121 46.546 1.00 35.90 B ATOM 2232 CB LYS B 412 52.537 6.742 46.595 1.00 35.46 B ATOM 2233 CG LYS B 412 52.373 7.994 47.470 1.00 34.91 B ATOM 2234 CD LYS B 412 53.251 9.163 47.023 1.00 33.80 B ATOM 2235 CE LYS B 412 52.905 10.407 47.809 1.00 32.17 B ATOM 2236 NZ LYS B 412 53.762 11.553 47.463 1.00 32.35 B ATOM 2237 C LYS B 412 53.812 4.629 46.256 1.00 35.57 B ATOM 2238 O LYS B 412 52.703 4.092 46.252 1.00 35.07 B ATOM 2239 N LYS B 413 54.932 3.959 46.007 1.00 35.95 B ATOM 2240 CA LYS B 413 54.901 2.523 45.721 1.00 36.16 B ATOM 2241 CB LYS B 413 54.977 2.254 44.205 1.00 36.93 B ATOM 2242 CG LYS B 413 53.730 2.627 43.387 1.00 40.07 B ATOM 2243 CD LYS B 413 53.913 2.308 41.900 1.00 41.03 B ATOM 2244 CE LYS B 413 52.629 2.529 41.105 1.00 42.27 B ATOM 2245 NZ LYS B 413 51.504 1.699 41.610 1.00 43.62 B ATOM 2246 C LYS B 413 56.047 1.798 46.402 1.00 35.81 B ATOM 2247 O LYS B 413 57.012 2.417 46.841 1.00 33.26 B ATOM 2248 N PHE B 414 55.904 0.481 46.503 1.00 38.03 B ATOM 2249 CA PHE B 414 56.909 −0.402 47.090 1.00 39.76 B ATOM 2250 CB PHE B 414 56.267 −1.749 47.454 1.00 40.36 B ATOM 2251 CG PHE B 414 57.257 −2.806 47.872 1.00 42.43 B ATOM 2252 CD1 PHE B 414 57.994 −2.667 49.046 1.00 43.87 B ATOM 2253 CD2 PHE B 414 57.499 −3.914 47.058 1.00 41.81 B ATOM 2254 CE1 PHE B 414 58.965 −3.614 49.398 1.00 43.95 B ATOM 2255 CE2 PHE B 414 58.466 −4.863 47.401 1.00 41.35 B ATOM 2256 CZ PHE B 414 59.201 −4.712 48.571 1.00 42.36 B ATOM 2257 C PHE B 414 57.970 −0.598 46.003 1.00 40.17 B ATOM 2258 O PHE B 414 57.642 −0.894 44.854 1.00 39.12 B ATOM 2259 N LEU B 415 59.236 −0.425 46.361 1.00 41.37 B ATOM 2260 CA LEU B 415 60.305 −0.558 45.386 1.00 42.80 B ATOM 2261 CB LEU B 415 61.350 0.539 45.608 1.00 44.70 B ATOM 2262 CG LEU B 415 62.211 0.891 44.391 1.00 46.65 B ATOM 2263 CD1 LEU B 415 61.335 1.453 43.273 1.00 46.10 B ATOM 2264 CD2 LEU B 415 63.277 1.905 44.794 1.00 47.87 B ATOM 2265 C LEU B 415 60.950 −1.941 45.464 1.00 43.04 B ATOM 2266 O LEU B 415 60.930 −2.699 44.503 1.00 42.67 B ATOM 2267 N LEU B 416 61.531 −2.288 46.600 1.00 43.99 B ATOM 2268 CA LEU B 416 62.140 −3.607 46.711 1.00 44.67 B ATOM 2269 CB LEU B 416 63.471 −3.667 45.948 1.00 43.56 B ATOM 2270 CG LEU B 416 64.709 −3.198 46.703 1.00 42.12 B ATOM 2271 CD1 LEU B 416 65.621 −4.380 46.873 1.00 45.95 B ATOM 2272 CD2 LEU B 416 65.421 −2.101 45.951 1.00 41.53 B ATOM 2273 C LEU B 416 62.363 −3.960 48.165 1.00 44.94 B ATOM 2274 O LEU B 416 62.183 −3.123 49.060 1.00 45.50 B ATOM 2275 N GLN B 417 62.747 −5.212 48.393 1.00 45.21 B ATOM 2276 CA GLN B 417 62.999 −5.712 49.744 1.00 45.08 B ATOM 2277 CB GLN B 417 61.984 −6.808 50.120 1.00 43.81 B ATOM 2278 CG GLN B 417 62.106 −7.321 51.555 1.00 40.41 B ATOM 2279 CD GLN B 417 61.077 −8.383 51.890 1.00 39.74 B ATOM 2280 OE1 GLN B 417 61.135 −9.507 51.390 1.00 41.92 B ATOM 2281 NE2 GLN B 417 60.129 −8.033 52.741 1.00 38.39 B ATOM 2282 C GLN B 417 64.412 −6.279 49.844 1.00 44.86 B ATOM 2283 O GLN B 417 64.906 −6.895 48.897 1.00 43.18 B ATOM 2284 N LEU B 418 65.053 −6.053 50.991 1.00 45.20 B ATOM 2285 CA LEU B 418 66.408 −6.536 51.246 1.00 44.82 B ATOM 2286 CB LEU B 418 67.329 −5.373 51.654 1.00 42.07 B ATOM 2287 CG LEU B 418 67.665 −4.358 50.550 1.00 40.04 B ATOM 2288 CD1 LEU B 418 67.984 −2.989 51.123 1.00 38.25 B ATOM 2289 CD2 LEU B 418 68.804 −4.885 49.746 1.00 39.20 B ATOM 2290 C LEU B 418 66.337 −7.584 52.357 1.00 46.53 B ATOM 2291 O LEU B 418 65.728 −7.355 53.411 1.00 46.91 B ATOM 2292 N SER B 419 66.929 −8.747 52.086 1.00 47.50 B ATOM 2293 CA SER B 419 66.966 −9.854 53.037 1.00 47.26 B ATOM 2294 CB SER B 419 66.219 −11.066 52.489 1.00 47.58 B ATOM 2295 OG SER B 419 66.861 −11.552 51.330 1.00 47.48 B ATOM 2296 C SER B 419 68.423 −10.219 53.282 1.00 47.06 B ATOM 2297 O SER B 419 69.267 −10.064 52.396 1.00 46.04 B ATOM 2298 N GLY B 420 68.700 −10.697 54.493 1.00 47.22 B ATOM 2299 CA GLY B 420 70.047 −11.059 54.886 1.00 46.53 B ATOM 2300 C GLY B 420 70.121 −11.386 56.366 1.00 47.16 B ATOM 2301 O GLY B 420 70.335 −12.546 56.715 1.00 48.39 B ATOM 2302 N HIS B 421 69.927 −10.390 57.237 1.00 46.12 B ATOM 2303 CA HIS B 421 69.999 −10.611 58.697 1.00 44.26 B ATOM 2304 CB HIS B 421 69.340 −9.451 59.469 1.00 42.53 B ATOM 2305 CG HIS B 421 70.144 −8.187 59.459 1.00 41.48 B ATOM 2306 CD2 HIS B 421 70.083 −7.102 58.653 1.00 41.32 B ATOM 2307 ND1 HIS B 421 71.231 −7.991 60.282 1.00 41.41 B ATOM 2308 CE1 HIS B 421 71.811 −6.845 59.977 1.00 41.09 B ATOM 2309 NE2 HIS B 421 71.135 −6.286 58.990 1.00 40.64 B ATOM 2310 C HIS B 421 69.374 −11.937 59.142 1.00 44.07 B ATOM 2311 O HIS B 421 68.254 −12.277 58.746 1.00 43.02 B ATOM 2312 N ASP B 422 70.103 −12.687 59.964 1.00 43.55 B ATOM 2313 CA ASP B 422 69.599 −13.967 60.447 1.00 43.78 B ATOM 2314 CB ASP B 422 70.752 −14.881 60.881 1.00 46.42 B ATOM 2315 CG ASP B 422 71.843 −15.013 59.811 1.00 48.64 B ATOM 2316 OD1 ASP B 422 71.518 −15.368 58.649 1.00 47.48 B ATOM 2317 OD2 ASP B 422 73.030 −14.762 60.145 1.00 50.00 B ATOM 2318 C ASP B 422 68.634 −13.762 61.609 1.00 42.50 B ATOM 2319 O ASP B 422 67.970 −14.701 62.048 1.00 41.14 B ATOM 2320 N GLY B 423 68.561 −12.527 62.099 1.00 42.77 B ATOM 2321 CA GLY B 423 67.659 −12.192 63.195 1.00 42.60 B ATOM 2322 C GLY B 423 66.843 −10.950 62.865 1.00 41.88 B ATOM 2323 O GLY B 423 67.107 −10.300 61.855 1.00 42.25 B ATOM 2324 N GLY B 424 65.854 −10.615 63.694 1.00 41.87 B ATOM 2325 CA GLY B 424 65.036 −9.432 63.433 1.00 41.62 B ATOM 2326 C GLY B 424 65.863 −8.158 63.492 1.00 41.35 B ATOM 2327 O GLY B 424 66.673 −7.994 64.389 1.00 41.29 B ATOM 2328 N VAL B 425 65.682 −7.254 62.541 1.00 41.10 B ATOM 2329 CA VAL B 425 66.452 −6.015 62.557 1.00 42.45 B ATOM 2330 CB VAL B 425 66.622 −5.464 61.137 1.00 44.73 B ATOM 2331 CG1 VAL B 425 65.322 −5.641 60.365 1.00 45.42 B ATOM 2332 CG2 VAL B 425 67.028 −3.987 61.187 1.00 45.68 B ATOM 2333 C VAL B 425 65.796 −4.946 63.433 1.00 41.72 B ATOM 2334 O VAL B 425 64.600 −4.702 63.318 1.00 42.42 B ATOM 2335 N TRP B 426 66.575 −4.305 64.301 1.00 40.55 B ATOM 2336 CA TRP B 426 66.016 −3.284 65.177 1.00 39.71 B ATOM 2337 CB TRP B 426 66.069 −3.755 66.632 1.00 36.69 B ATOM 2338 CG TRP B 426 65.117 −4.874 66.920 1.00 34.11 B ATOM 2339 CD2 TRP B 426 63.831 −4.774 67.558 1.00 32.48 B ATOM 2340 CE2 TRP B 426 63.275 −6.072 67.578 1.00 30.88 B ATOM 2341 CE3 TRP B 426 63.098 −3.715 68.110 1.00 30.22 B ATOM 2342 CD1 TRP B 426 65.278 −6.185 66.594 1.00 33.27 B ATOM 2343 NE1 TRP B 426 64.179 −6.910 66.984 1.00 32.30 B ATOM 2344 CZ2 TRP B 426 62.017 −6.344 68.129 1.00 31.05 B ATOM 2345 CZ3 TRP B 426 61.845 −3.984 68.661 1.00 30.71 B ATOM 2346 CH2 TRP B 426 61.319 −5.289 68.666 1.00 30.24 B ATOM 2347 C TRP B 426 66.631 −1.889 65.066 1.00 40.31 B ATOM 2348 O TRP B 426 66.089 −0.930 65.607 1.00 40.76 B ATOM 2349 N ALA B 427 67.759 −1.774 64.379 1.00 41.09 B ATOM 2350 CA ALA B 427 68.400 −0.482 64.198 1.00 42.24 B ATOM 2351 CB ALA B 427 69.783 −0.481 64.816 1.00 42.58 B ATOM 2352 C ALA B 427 68.488 −0.284 62.695 1.00 43.39 B ATOM 2353 O ALA B 427 68.658 −1.251 61.952 1.00 44.01 B ATOM 2354 N LEU B 428 68.375 0.963 62.248 1.00 44.59 B ATOM 2355 CA LEU B 428 68.401 1.261 60.821 1.00 44.89 B ATOM 2356 CB LEU B 428 67.015 0.996 60.230 1.00 45.56 B ATOM 2357 CG LEU B 428 66.894 0.895 58.717 1.00 46.48 B ATOM 2358 CD1 LEU B 428 67.730 −0.281 58.221 1.00 47.28 B ATOM 2359 CD2 LEU B 428 65.434 0.710 58.349 1.00 46.47 B ATOM 2360 C LEU B 428 68.761 2.714 60.608 1.00 44.99 B ATOM 2361 O LEU B 428 68.132 3.596 61.178 1.00 46.41 B ATOM 2362 N LYS B 429 69.766 2.969 59.785 1.00 44.76 B ATOM 2363 CA LYS B 429 70.189 4.341 59.519 1.00 44.20 B ATOM 2364 CB LYS B 429 71.478 4.631 60.288 1.00 43.86 B ATOM 2365 CG LYS B 429 72.022 6.021 60.108 1.00 43.02 B ATOM 2366 CD LYS B 429 71.151 7.060 60.779 1.00 40.87 B ATOM 2367 CE LYS B 429 71.741 8.447 60.560 1.00 38.32 B ATOM 2368 NZ LYS B 429 71.164 9.464 61.464 1.00 34.95 B ATOM 2369 C LYS B 429 70.406 4.457 58.021 1.00 44.44 B ATOM 2370 O LYS B 429 70.534 3.445 57.344 1.00 44.65 B ATOM 2371 N TYR B 430 70.430 5.677 57.496 1.00 45.98 B ATOM 2372 CA TYR B 430 70.617 5.884 56.052 1.00 46.60 B ATOM 2373 CB TYR B 430 69.403 6.616 55.458 1.00 43.95 B ATOM 2374 CG TYR B 430 69.496 6.911 53.973 1.00 41.46 B ATOM 2375 CD1 TYR B 430 69.092 5.976 53.027 1.00 40.19 B ATOM 2376 CE1 TYR B 430 69.153 6.255 51.664 1.00 38.85 B ATOM 2377 CD2 TYR B 430 69.968 8.137 53.520 1.00 40.10 B ATOM 2378 CE2 TYR B 430 70.034 8.430 52.164 1.00 39.82 B ATOM 2379 CZ TYR B 430 69.625 7.486 51.232 1.00 39.47 B ATOM 2380 OH TYR B 430 69.691 7.784 49.874 1.00 37.41 B ATOM 2381 C TYR B 430 71.872 6.696 55.767 1.00 47.43 B ATOM 2382 O TYR B 430 72.320 7.476 56.603 1.00 48.99 B ATOM 2383 N ALA B 431 72.439 6.516 54.582 1.00 48.65 B ATOM 2384 CA ALA B 431 73.634 7.263 54.196 1.00 48.95 B ATOM 2385 CB ALA B 431 74.882 6.412 54.420 1.00 49.04 B ATOM 2386 C ALA B 431 73.533 7.683 52.732 1.00 49.00 B ATOM 2387 O ALA B 431 73.298 6.860 51.842 1.00 48.35 B ATOM 2388 N HIS B 432 73.729 8.967 52.482 1.00 49.81 B ATOM 2389 CA HIS B 432 73.627 9.485 51.126 1.00 52.51 B ATOM 2390 CB HIS B 432 74.421 10.787 50.978 1.00 55.86 B ATOM 2391 CG HIS B 432 74.148 11.508 49.695 1.00 60.52 B ATOM 2392 CD2 HIS B 432 74.984 12.012 48.757 1.00 62.00 B ATOM 2393 ND1 HIS B 432 72.869 11.750 49.238 1.00 62.73 B ATOM 2394 CE1 HIS B 432 72.930 12.368 48.072 1.00 63.55 B ATOM 2395 NE2 HIS B 432 74.202 12.539 47.757 1.00 63.41 B ATOM 2396 C HIS B 432 74.084 8.497 50.059 1.00 51.80 B ATOM 2397 O HIS B 432 75.031 7.737 50.266 1.00 53.10 B ATOM 2398 N GLY B 433 73.391 8.508 48.923 1.00 50.58 B ATOM 2399 CA GLY B 433 73.741 7.633 47.819 1.00 47.93 B ATOM 2400 C GLY B 433 72.921 6.368 47.714 1.00 47.35 B ATOM 2401 O GLY B 433 73.272 5.462 46.963 1.00 47.94 B ATOM 2402 N GLY B 434 71.823 6.293 48.452 1.00 46.94 B ATOM 2403 CA GLY B 434 71.016 5.090 48.392 1.00 45.51 B ATOM 2404 C GLY B 434 71.722 3.980 49.147 1.00 44.93 B ATOM 2405 O GLY B 434 71.599 2.804 48.824 1.00 45.17 B ATOM 2406 N ILE B 435 72.501 4.353 50.151 1.00 44.36 B ATOM 2407 CA ILE B 435 73.183 3.352 50.943 1.00 43.99 B ATOM 2408 CB ILE B 435 74.701 3.520 50.874 1.00 43.64 B ATOM 2409 CG2 ILE B 435 75.375 2.722 51.989 1.00 43.26 B ATOM 2410 CG1 ILE B 435 75.196 3.022 49.528 1.00 43.31 B ATOM 2411 CD1 ILE B 435 76.656 3.223 49.321 1.00 45.00 B ATOM 2412 C ILE B 435 72.724 3.435 52.395 1.00 44.68 B ATOM 2413 O ILE B 435 72.570 4.518 52.956 1.00 42.73 B ATOM 2414 N LEU B 436 72.486 2.283 53.000 1.00 44.69 B ATOM 2415 CA LEU B 436 72.051 2.273 54.376 1.00 46.18 B ATOM 2416 CB LEU B 436 70.545 2.006 54.468 1.00 46.74 B ATOM 2417 CG LEU B 436 70.020 0.623 54.084 1.00 46.70 B ATOM 2418 CD1 LEU B 436 68.660 0.398 54.708 1.00 47.92 B ATOM 2419 CD2 LEU B 436 69.953 0.506 52.574 1.00 48.12 B ATOM 2420 C LEU B 436 72.816 1.224 55.176 1.00 47.09 B ATOM 2421 O LEU B 436 73.360 0.268 54.619 1.00 46.99 B ATOM 2422 N VAL B 437 72.862 1.418 56.488 1.00 46.98 B ATOM 2423 CA VAL B 437 73.552 0.497 57.376 1.00 48.04 B ATOM 2424 CB VAL B 437 74.617 1.244 58.228 1.00 49.43 B ATOM 2425 CG1 VAL B 437 75.517 0.251 58.948 1.00 48.59 B ATOM 2426 CG2 VAL B 437 75.443 2.180 57.333 1.00 49.25 B ATOM 2427 C VAL B 437 72.481 −0.062 58.299 1.00 46.89 B ATOM 2428 O VAL B 437 71.430 0.551 58.449 1.00 47.34 B ATOM 2429 N SER B 438 72.722 −1.222 58.902 1.00 45.63 B ATOM 2430 CA SER B 438 71.741 −1.788 59.820 1.00 44.89 B ATOM 2431 CB SER B 438 70.729 −2.644 59.072 1.00 44.08 B ATOM 2432 OG SER B 438 71.355 −3.758 58.467 1.00 44.83 B ATOM 2433 C SER B 438 72.377 −2.622 60.914 1.00 44.82 B ATOM 2434 O SER B 438 73.561 −2.949 60.857 1.00 44.21 B ATOM 2435 N GLY B 439 71.568 −2.945 61.916 1.00 45.02 B ATOM 2436 CA GLY B 439 72.020 ‘3.751 63.027 1.00 45.90 B ATOM 2437 C GLY B 439 70.855 −4.596 63.498 1.00 46.75 B ATOM 2438 O GLY B 439 69.809 −4.054 63.843 1.00 45.99 B ATOM 2439 N SER B 440 71.006 −5.915 63.496 1.00 49.24 B ATOM 2440 CA SER B 440 69.919 −6.773 63.957 1.00 53.65 B ATOM 2441 CB SER B 440 69.429 −7.707 62.842 1.00 54.51 B ATOM 2442 OG SER B 440 70.342 −8.766 62.610 1.00 56.40 B ATOM 2443 C SER B 440 70.368 −7.612 65.146 1.00 54.82 B ATOM 2444 O SER B 440 71.474 −7.447 65.660 1.00 54.64 B ATOM 2445 N T5R B 441 69.490 −8.509 65.576 1.00 57.06 B ATOM 2446 CA THR B 441 69.769 −9.392 66.695 1.00 59.13 B ATOM 2447 CB THR B 441 68.498 −10.086 67.165 1.00 57.43 B ATOM 2448 OG1 THR B 441 67.489 −9.101 67.397 1.00 55.10 B ATOM 2449 CG2 THR B 441 68.761 −10.835 68.455 1.00 59.62 B ATOM 2450 C T5R B 441 70.778 −10.442 66.262 1.00 61.73 B ATOM 2451 O THR B 441 71.212 −11.280 67.048 1.00 62.25 B ATOM 2452 N ASP B 442 71.142 −10.379 64.989 1.00 64.11 B ATOM 2453 CA ASP B 442 72.098 −11.292 64.403 1.00 65.34 B ATOM 2454 CB ASP B 442 72.028 −11.183 62.877 1.00 69.79 B ATOM 2455 CG ASP B 442 72.888 −12.220 62.171 1.00 76.04 B ATOM 2456 OD1 ASP B 442 72.837 −13.413 62.567 1.00 78.67 B ATOM 2457 OD2 ASP B 442 73.607 −11.846 61.208 1.00 78.25 B ATOM 2458 C ASP B 442 73.490 −10.929 64.903 1.00 64.29 B ATOM 2459 O ASP B 442 74.469 −11.621 64.626 1.00 65.24 B ATOM 2460 N ARG B 443 73.561 −9.843 65.662 1.00 62.52 B ATOM 2461 CA ARG B 443 74.817 −9.346 66.214 1.00 60.60 B ATOM 2462 CB ARG B 443 75.495 −10.412 67.088 1.00 61.78 B ATOM 2463 CG ARG B 443 74.629 −10.891 68.231 1.00 64.13 B ATOM 2464 CD ARG B 443 75.329 −11.918 69.100 1.00 65.45 B ATOM 2465 NE ARG B 443 75.805 −13.045 68.312 1.00 68.14 B ATOM 2466 CZ ARG B 443 76.062 −14.252 68.804 1.00 69.90 B ATOM 2467 NH1 ARG B 443 75.885 −14.495 70.096 1.00 69.79 B ATOM 2468 NH2 ARG B 443 76.493 −15.219 67.998 1.00 70.62 B ATOM 2469 C ARG B 443 75.754 −8.904 65.100 1.00 58.12 B ATOM 2470 O ARG B 443 76.972 −8.886 65.266 1.00 58.34 B ATOM 2471 N THR B 444 75.183 −8.534 63.960 1.00 55.54 B ATOM 2472 CA THR B 444 76.005 −8.092 62.841 1.00 53.90 B ATOM 2473 CB THR B 444 75.945 −9.106 61.671 1.00 54.03 B ATOM 2474 OG1 THR B 444 74.590 −9.262 61.232 1.00 53.30 B ATOM 2475 CG2 THR B 444 76.482 −10.464 62.113 1.00 53.83 B ATOM 2476 C THR B 444 75.567 −6.727 62.338 1.00 51.81 B ATOM 2477 O THR B 444 74.401 −6.377 62.409 1.00 52.22 B ATOM 2478 N VAL B 445 76.510 −5.945 61.846 1.00 49.88 B ATOM 2479 CA VAL B 445 76.169 −4.641 61.330 1.00 49.27 B ATOM 2480 CB VAL B 445 77.158 −3.569 61.825 1.00 48.34 B ATOM 2481 CG1 VAL B 445 76.756 −2.196 61.303 1.00 47.11 B ATOM 2482 CG2 VAL B 445 77.192 −3.566 63.349 1.00 48.46 B ATOM 2483 C VAL B 445 76.233 −4.745 59.813 1.00 50.36 B ATOM 2484 O VAL B 445 77.308 −4.656 59.209 1.00 50.35 B ATOM 2485 N ARG B 446 75.080 −4.959 59.194 1.00 50.86 B ATOM 2486 CA ARG B 446 75.039 −5.081 57.749 1.00 51.42 B ATOM 2487 CB ARG B 446 74.024 −6.152 57.329 1.00 52.81 B ATOM 2488 CG ARG B 446 74.384 −7.595 57.725 1.00 53.32 B ATOM 2489 CD ARG B 446 73.563 −8.565 56.893 1.00 54.70 B ATOM 2490 NE ARG B 446 73.801 −9.970 57.206 1.00 55.46 B ATOM 2491 CZ ARG B 446 73.462 −10.545 58.353 1.00 57.14 B ATOM 2492 NH1 ARG B 446 72.878 −9.834 59.303 1.00 59.85 B ATOM 2493 NH2 ARG B 446 73.677 −11.839 58.548 1.00 57.51 B ATOM 2494 C ARG B 446 74.712 −3.759 57.058 1.00 50.94 B ATOM 2495 O ARG B 446 73.764 −3.066 57.427 1.00 51.11 B ATOM 2496 N VAL B 447 75.525 −3.414 56.063 1.00 49.98 B ATOM 2497 CA VAL B 447 75.338 −2.198 55.280 1.00 49.12 B ATOM 2498 CB VAL B 447 76.661 −1.360 55.196 1.00 49.77 B ATOM 2499 CG1 VAL B 447 77.858 −2.268 55.110 1.00 48.80 B ATOM 2500 CG2 VAL B 447 76.631 −0.433 53.984 1.00 50.29 B ATOM 2501 C VAL B 447 74.876 −2.650 53.893 1.00 47.59 B ATOM 2502 O VAL B 447 75.433 −3.584 53.334 1.00 46.28 B ATOM 2503 N TRP B 448 73.841 −2.001 53.361 1.00 47.07 B ATOM 2504 CA TRP B 448 73.278 −2.349 52.058 1.00 46.70 B ATOM 2505 CB TRP B 448 71.807 −2.704 52.201 1.00 43.15 B ATOM 2506 CG TRP B 448 71.506 −3.423 53.437 1.00 40.87 B ATOM 2507 CD2 TRP B 448 71.126 −4.793 53.554 1.00 39.93 B ATOM 2508 CE2 TRP B 448 70.984 −5.067 54.925 1.00 39.42 B ATOM 2509 CE3 TRP B 448 70.907 −5.820 52.635 1.00 38.21 B ATOM 2510 CD1 TRP B 448 71.565 −2.930 54.698 1.00 40.70 B ATOM 2511 NE1 TRP B 448 71.253 −3.910 55.603 1.00 40.18 B ATOM 2512 CZ2 TRP B 448 70.620 −6.324 55.400 1.00 39.77 B ATOM 2513 CZ3 TRP B 448 70.547 −7.073 53.110 1.00 38.97 B ATOM 2514 CH2 TRP B 448 70.413 −7.314 54.480 1.00 38.38 B ATOM 2515 C TRP B 448 73.383 −1.223 51.038 1.00 48.93 B ATOM 2516 O TRP B 448 73.774 −0.096 51.360 1.00 49.67 B ATOM 2517 N ASP B 449 73.001 −1.542 49.803 1.00 51.05 B ATOM 2518 CA ASP B 449 73.014 −0.586 48.698 1.00 52.47 B ATOM 2519 CB ASP B 449 74.247 −0.830 47.826 1.00 53.58 B ATOM 2520 CG ASP B 449 74.259 0.024 46.568 1.00 55.71 B ATOM 2521 OD1 ASP B 449 73.432 −0.234 45.662 1.00 56.14 B ATOM 2522 OD2 ASP B 449 75.095 0.954 46.489 1.00 55.67 B ATOM 2523 C ASP B 449 71.733 −0.750 47.867 1.00 52.24 B ATOM 2524 O ASP B 449 71.541 −1.777 47.225 1.00 52.13 B ATOM 2525 N ILE B 450 70.864 0.260 47.883 1.00 52.28 B ATOM 2526 CA ILE B 450 69.607 0.199 47.135 1.00 52.23 B ATOM 2527 CB ILE B 450 68.729 1.477 47.359 1.00 51.25 B ATOM 2528 CG2 ILE B 450 67.411 1.352 46.609 1.00 50.40 B ATOM 2529 CG1 ILE B 450 68.430 1.658 48.851 1.00 50.03 B ATOM 2530 CO1 ILE B 450 67.617 2.890 49.180 1.00 49.00 B ATOM 2531 C ILE B 450 69.849 0.024 45.639 1.00 52.47 B ATOM 2532 O ILE B 450 69.266 −0.860 45.024 1.00 52.87 B ATOM 2533 N LYS B 451 70.705 0.863 45.060 1.00 53.03 B ATOM 2534 CA LYS B 451 71.008 0.779 43.638 1.00 53.15 B ATOM 2535 CB LYS B 451 72.346 1.458 43.339 1.00 53.71 B ATOM 2536 CG LYS B 451 72.315 2.978 43.471 0.00 54.77 B ATOM 2537 CD LYS B 451 71.228 3.578 42.581 0.00 55.27 B ATOM 2538 CE LYS B 451 71.190 5.104 42.643 0.00 55.45 B ATOM 2539 NZ LYS B 451 72.286 5.761 41.877 0.00 55.61 B ATOM 2540 C LYS B 451 71.059 −0.684 43.212 1.00 53.22 B ATOM 2541 O LYS B 451 70.241 −1.139 42.415 1.00 51.85 B ATOM 2542 N LYS B 452 72.007 −1.428 43.765 1.00 54.30 B ATOM 2543 CA LYS B 452 72.138 −2.833 43.431 1.00 55.55 B ATOM 2544 CB LYS B 452 73.549 −3.321 43.756 1.00 56.49 B ATOM 2545 CG LYS B 452 74.596 −2.840 42.773 0.00 57.18 B ATOM 2546 CD LYS B 452 74.345 −3.420 41.393 0.00 57.78 B ATOM 2547 CE LYS B 452 75.353 −2.896 40.391 0.00 58.13 B ATOM 2548 NZ LYS B 452 75.066 −3.409 39.027 0.00 58.45 B ATOM 2549 C LYS B 452 71.113 −3.701 44.147 1.00 56.44 B ATOM 2550 O LYS B 452 70.797 −4.790 43.679 1.00 58.17 B ATOM 2551 N GLY B 453 70.594 −3.234 45.279 1.00 56.96 B ATOM 2552 CA GLY B 453 69.605 −4.013 46.013 1.00 57.08 B ATOM 2553 C GLY B 453 70.167 −5.275 46.650 1.00 57.02 B ATOM 2554 O GLY B 453 69.573 −6.353 46.568 1.00 56.26 B ATOM 2555 N CYS B 454 71.319 −5.143 47.297 1.00 57.42 B ATOM 2556 CA CYS B 454 71.958 −6.281 47.945 1.00 57.82 B ATOM 2557 CB CYS B 454 72.844 −7.024 46.937 1.00 59.05 B ATOM 2558 SG CYS B 454 74.118 −5.986 46.135 1.00 59.80 B ATOM 2559 C GY5 B 454 72.800 −5.834 49.136 1.00 57.12 B ATOM 2560 O CYS B 454 73.084 −4.644 49.300 1.00 57.22 B ATOM 2561 N CYS B 455 73.196 −6.798 49.961 1.00 55.66 B ATOM 2562 CA CYS B 455 74.021 −6.529 51.136 1.00 54.95 B ATOM 2563 CB CYS B 455 73.831 −7.667 52.140 1.00 54.92 B ATOM 2564 SG GY5 B 455 74.504 −7.375 53.769 1.00 58.03 B ATOM 2565 C GY5 B 455 75.485 −6.436 50.678 1.00 54.21 B ATOM 2566 O CYS B 455 76.024 −7.404 50.146 1.00 55.39 B ATOM 2567 N THR B 456 76.120 −5.277 50.875 1.00 52.48 B ATOM 2568 CA THR B 456 77.514 −5.074 50.446 1.00 50.81 B ATOM 2569 CB THR B 456 77.771 −3.609 49.987 1.00 50.32 B ATOM 2570 OG1 THR B 456 77.631 −2.712 51.095 1.00 50.40 B ATOM 2571 CG2 THR B 456 76.808 −3.217 48.894 1.00 49.71 B ATOM 2572 C THR B 456 78.608 −5.434 51.472 1.00 49.16 B ATOM 2573 O THR B 456 79.773 −5.613 51.109 1.00 49.26 B ATOM 2574 N HIS B 457 78.242 −5.537 52.743 1.00 46.55 B ATOM 2575 CA HIS B 457 79.205 −5.871 53.780 1.00 43.83 B ATOM 2576 CB HIS B 457 79.956 −4.615 54.229 1.00 43.71 B ATOM 2577 CG HIS B 457 80.731 −3.947 53.136 1.00 44.34 B ATOM 2578 CD2 HIS B 457 80.557 −2.753 52.524 1.00 44.60 B ATOM 2579 ND1 HIS B 457 81.832 −4.524 52.543 1.00 44.61 B ATOM 2580 CE1 HIS B 457 82.305 −3.711 51.615 1.00 44.83 B ATOM 2581 NE2 HIS B 457 81.550 −2.630 51.584 1.00 43.67 B ATOM 2582 C HIS B 457 78.512 −6.512 54.979 1.00 42.72 B ATOM 2583 O HIS B 457 77.307 −6.342 55.178 1.00 41.66 B ATOM 2584 N VAL B 458 79.275 −7.255 55.776 1.00 42.43 B ATOM 2585 CA VAL B 458 78.725 −7.918 56.958 1.00 40.96 B ATOM 2586 CB VAL B 458 78.386 −9.383 56.655 1.00 41.12 B ATOM 2587 CG1 VAL B 458 77.331 −9.883 57.628 1.00 39.96 B ATOM 2588 CG2 VAL B 458 77.913 −9.519 55.225 1.00 40.46 B ATOM 2589 C VAL B 458 79.711 −7.852 58.130 1.00 39.97 B ATOM 2590 O VAL B 458 80.391 −8.820 58.456 1.00 38.56 B ATOM 2591 N PHE B 459 79.744 −6.690 58.768 1.00 40.60 B ATOM 2592 CA PHE B 459 80.623 −6.413 59.892 1.00 41.18 B ATOM 2593 CB PHE B 459 80.675 −4.901 60.084 1.00 38.09 B ATOM 2594 CG PHE B 459 81.196 −4.158 58.881 1.00 36.10 B ATOM 2595 CD1 PHE B 459 81.182 −2.765 58.850 1.00 34.95 B ATOM 2596 CD2 PHE B 459 81.767 −4.847 57.813 1.00 34.29 B ATOM 2597 CE1 PHE B 459 81.741 −2.055 57.773 1.00 34.55 B ATOM 2598 CE2 PHE B 459 82.328 −4.160 56.734 1.00 35.73 B ATOM 2599 CZ PHE B 459 82.317 −2.755 56.713 1.00 36.03 B ATOM 2600 C PHE B 459 80.237 −7.104 61.209 1.00 43.45 B ATOM 2601 O PHE B 459 79.357 −6.630 61.921 1.00 44.50 B ATOM 2602 N GLU B 460 80.900 −8.216 61.538 1.00 46.24 B ATOM 2603 CA GLU B 460 80.608 −8.939 62.783 1.00 47.21 B ATOM 2604 CB GLU B 460 80.750 −10.456 62.599 1.00 46.96 B ATOM 2605 CG GLU B 460 79.920 −11.030 61.473 1.00 51.03 B ATOM 2606 CD GLU B 460 79.971 −12.553 61.386 1.00 52.17 B ATOM 2607 OE1 GLU B 460 81.079 −13.110 61.261 1.00 54.35 B ATOM 2608 OE2 GLU B 460 78.897 −13.194 61.428 1.00 51.82 B ATOM 2609 C GLU B 460 81.532 −8.491 63.909 1.00 47.31 B ATOM 2610 O GUI B 460 82.567 −7.863 63.674 1.00 45.71 B ATOM 2611 N GLY B 461 81.147 −8.835 65.134 1.00 48.17 B ATOM 2612 CA GLY B 461 81.928 −8.456 66.292 1.00 49.82 B ATOM 2613 C GLY B 461 81.102 −8.363 67.561 1.00 50.83 B ATOM 2614 O GLY B 461 81.379 −9.074 68.529 1.00 50.20 B ATOM 2615 N HIS B 462 80.086 −7.501 67.565 1.00 51.06 B ATOM 2616 CA HIS B 462 79.251 −7.346 68.750 1.00 51.73 B ATOM 2617 CB HIS B 462 78.010 −6.487 68.443 1.00 50.07 B ATOM 2618 CG HIS B 462 78.284 −5.011 68.421 1.00 48.90 B ATOM 2619 CD2 HIS B 462 78.451 −4.151 67.388 1.00 48.64 B ATOM 2620 ND1 HIS B 462 78.443 −4.264 69.568 1.00 49.43 B ATOM 2621 CE1 HIS B 462 78.697 −3.009 69.242 1.00 50.51 B ATOM 2622 NE2 HIS B 462 78.708 −2.914 67.925 1.00 48.70 B ATOM 2623 C HIS B 462 78.846 −8.707 69.315 1.00 52.82 B ATOM 2624 O HIS B 462 78.076 −9.459 68.704 1.00 53.62 B ATOM 2625 N ASN B 463 79.394 −9.013 70.490 1.00 53.69 B ATOM 2626 CA ASN B 463 79.140 −10.269 71.186 1.00 53.67 B ATOM 2627 CB ASN B 463 80.119 −10.413 72.369 0.00 53.95 B ATOM 2628 CG ASN B 463 81.588 −10.299 71.945 1.00 54.43 B ATOM 2629 OD1 ASN B 463 82.173 −11.235 71.378 1.00 55.63 B ATOM 2630 ND2 ASN B 463 82.184 −9.140 72.216 1.00 52.98 B ATOM 2631 C ASN B 463 77.699 −10.312 71.686 1.00 53.05 B ATOM 2632 O ASN B 463 77.353 −11.133 72.525 1.00 53.74 B ATOM 2633 N SER B 464 76.867 −9.414 71.162 1.00 53.52 B ATOM 2634 CA SER B 464 75.455 −9.330 71.540 1.00 51.56 B ATOM 2635 CB SER B 464 75.324 −8.732 72.946 1.00 52.15 B ATOM 2636 OG SER B 464 74.010 −8.925 73.444 1.00 54.03 B ATOM 2637 C SER B 464 74.645 −8.487 70.527 1.00 49.85 B ATOM 2638 O SER B 464 75.210 −7.852 69.622 1.00 47.81 B ATOM 2639 N THR B 465 73.321 −8.496 70.695 1.00 48.25 B ATOM 2640 CA THR B 465 72.390 −7.767 69.824 1.00 47.13 B ATOM 2641 CB THR B 465 70.924 −7.847 70.344 1.00 48.31 B ATOM 2642 OG1 THR B 465 70.510 −9.214 70.418 1.00 51.43 B ATOM 2643 CG2 THR B 465 69.971 −7.098 69.412 1.00 49.57 B ATOM 2644 C THR B 465 72.734 −6.292 69.669 1.00 45.19 B ATOM 2645 O THR B 465 73.067 −5.617 70.643 1.00 45.46 B ATOM 2646 N VAL B 466 72.636 −5.804 68.433 1.00 42.21 B ATOM 2647 CA VAL B 466 72.912 −4.406 68.125 1.00 39.22 B ATOM 2648 CB VAL B 466 73.293 −4.241 66.643 1.00 38.21 B ATOM 2649 CG1 VAL B 466 73.798 −2.829 66.378 1.00 37.18 B ATOM 2650 CG2 VAL B 466 74.354 −5.264 66.285 1.00 35.99 B ATOM 2651 C VAL B 466 71.626 −3.638 68.430 1.00 37.88 B ATOM 2652 O VAL B 466 70.655 −3.738 67.691 1.00 35.76 B ATOM 2653 N ARG B 467 71.623 −2.886 69.530 1.00 37.28 B ATOM 2654 CA ARG B 467 70.440 −2.145 69.938 1.00 36.20 B ATOM 2655 CB ARG B 467 70.399 −1.987 71.468 1.00 36.76 B ATOM 2656 CG ARG B 467 69.038 −1.513 72.012 1.00 36.98 B ATOM 2657 CD ARG B 467 67.945 −2.559 71.762 1.00 39.61 B ATOM 2658 NE ARG B 467 66.563 −2.103 71.979 1.00 40.08 B ATOM 2659 CZ ARG B 467 65.928 −1.213 71.220 1.00 38.58 B ATOM 2660 NH1 ARG B 467 66.539 −0.654 70.184 1.00 36.43 B ATOM 2661 NH2 ARG B 467 64.664 −0.913 71.476 1.00 39.24 B ATOM 2662 C ARG B 467 70.314 −0.773 69.283 1.00 35.21 B ATOM 2663 O ARG B 467 69.225 −0.213 69.247 1.00 36.67 B ATOM 2664 N CYS B 468 71.400 −0.222 68.758 1.00 33.04 B ATOM 2665 CA CYS B 468 71.304 1.088 68.127 1.00 33.09 B ATOM 2666 CB CYS B 468 71.069 2.167 69.186 1.00 32.72 B ATOM 2667 SG CYS B 468 72.414 2.394 70.339 1.00 34.24 B ATOM 2668 C CYS B 468 72.533 1.406 67.292 1.00 32.45 B ATOM 2669 O CYS B 468 73.473 0.618 67.263 1.00 33.24 B ATOM 2670 N LEU B 469 72.522 2.546 66.605 1.00 31.75 B ATOM 2671 CA LEU B 469 73.643 2.908 65.747 1.00 32.36 B ATOM 2672 CB LEU B 469 73.750 1.917 64.576 1.00 32.24 B ATOM 2673 CG LEU B 469 72.822 2.067 63.362 1.00 31.67 B ATOM 2674 CD1 LEU B 469 73.563 2.673 62.174 1.00 33.01 B ATOM 2675 CD2 LEU B 469 72.311 0.704 62.982 1.00 33.19 B ATOM 2676 C LEU B 469 73.491 4.309 65.179 1.00 32.21 B ATOM 2677 O LEU B 469 72.434 4.910 65.285 1.00 32.62 B ATOM 2678 N ASP B 470 74.552 4.833 64.581 1.00 33.12 B ATOM 2679 CA ASP B 470 74.481 6.149 63.972 1.00 34.33 B ATOM 2680 CB ASP B 470 74.431 7.223 65.055 1.00 33.47 B ATOM 2681 CG ASP B 470 74.098 8.585 64.501 1.00 32.01 B ATOM 2682 OD1 ASP B 470 73.302 8.647 63.551 1.00 35.18 B ATOM 2683 OD2 ASP B 470 74.614 9.589 65.021 1.00 29.33 B ATOM 2684 C ASP B 470 75.704 6.330 63.083 1.00 35.86 B ATOM 2685 O ASP B 470 76.619 5.509 63.124 1.00 36.56 B ATOM 2686 N ILE B 471 75.712 7.384 62.269 1.00 37.44 B ATOM 2687 CA ILE B 471 76.841 7.663 61.380 1.00 37.88 B ATOM 2688 CB ILE B 471 76.465 7.465 59.889 1.00 36.84 B ATOM 2689 CG2 ILE B 471 77.698 7.683 59.005 1.00 36.56 B ATOM 2690 CG1 ILE B 471 75.942 6.050 59.649 1.00 36.63 B ATOM 2691 CD1 ILE B 471 75.305 5.868 58.283 1.00 35.99 B ATOM 2692 C ILE B 471 77.309 9.106 61.569 1.00 38.95 B ATOM 2693 O ILE B 471 76.493 10.013 61.769 1.00 39.67 B ATOM 2694 N VAL B 472 78.625 9.305 61.522 1.00 39.62 B ATOM 2695 CA VAL B 472 79.219 10.631 61.670 1.00 40.41 B ATOM 2696 CB VAL B 472 79.932 10.786 63.018 1.00 39.84 B ATOM 2697 CG1 VAL B 472 78.967 10.468 64.158 1.00 37.97 B ATOM 2698 CG2 VAL B 472 81.150 9.862 63.066 1.00 38.84 B ATOM 2699 C VAL B 472 80.255 10.802 60.579 1.00 42.22 B ATOM 2700 O VAL B 472 80.780 9.820 60.064 1.00 41.41 B ATOM 2701 N GLU B 473 80.544 12.048 60.227 1.00 44.76 B ATOM 2702 CA GLU B 473 81.539 12.329 59.207 1.00 48.54 B ATOM 2703 CB GLU B 473 80.872 12.865 57.934 1.00 49.21 B ATOM 2704 CG GLU B 473 81.851 13.193 56.784 1.00 51.32 B ATOM 2705 CD GLU B 473 81.143 13.514 55.465 1.00 51.78 B ATOM 2706 OE1 GLU B 473 80.489 12.609 54.902 1.00 52.52 B ATOM 2707 OE2 GLU B 473 81.232 14.670 54.996 1.00 52.59 B ATOM 2708 C GLU B 473 82.568 13.329 59.737 1.00 50.91 B ATOM 2709 O GLU B 473 82.225 14.419 60.205 1.00 50.21 B ATOM 2710 N TYR B 474 83.835 12.933 59.683 1.00 53.85 B ATOM 2711 CA TYR B 474 84.927 13.775 60.151 1.00 56.31 B ATOM 2712 CB TYR B 474 85.504 13.214 61.450 1.00 57.48 B ATOM 2713 CG TYR B 474 86.410 14.180 62.164 1.00 59.70 B ATOM 2714 CD1 TYR B 474 85.925 15.408 62.613 1.00 60.47 B ATOM 2715 CE1 TYR B 474 86.744 16.305 63.285 1.00 60.97 B ATOM 2716 CD2 TYR B 474 87.749 13.870 62.402 1.00 60.68 B ATOM 2717 CE2 TYR B 474 88.581 14.763 63.075 1.00 61.50 B ATOM 2718 CZ TYR B 474 88.068 15.978 63.514 1.00 61.92 B ATOM 2719 OH TYR B 474 88.875 16.861 64.194 1.00 63.90 B ATOM 2720 C TYR B 474 86.001 13.795 59.075 1.00 56.54 B ATOM 2721 O TYR B 474 86.293 12.768 58.460 1.00 56.18 B ATOM 2722 N LYS B 475 86.589 14.966 58.856 1.00 58.01 B ATOM 2723 CA LYS B 475 87.623 15.128 57.840 1.00 59.54 B ATOM 2724 CB LYS B 475 88.958 14.579 58.351 1.00 60.12 B ATOM 2725 CG LYS B 475 89.453 15.213 59.653 1.00 60.74 B ATOM 2726 CD LYS B 475 89.934 16.642 59.449 1.00 61.48 B ATOM 2727 CE LYS B 475 90.341 17.283 60.765 0.00 61.92 B ATOM 2728 NZ LYS B 475 90.797 18.687 60.568 0.00 62.37 B ATOM 2729 C LYS B 475 87.200 14.393 56.563 1.00 60.31 B ATOM 2730 O LYS B 475 87.882 13.481 56.093 1.00 61.02 B ATOM 2731 N ASN B 476 86.057 14.796 56.020 1.00 60.89 B ATOM 2732 CA ASN B 476 85.523 14.199 54.813 1.00 60.87 B ATOM 2733 CB ASN B 476 86.260 14.759 53.594 1.00 63.50 B ATOM 2734 CG ASN B 476 85.792 16.172 53.224 1.00 66.46 B ATOM 2735 OD1 ASN B 476 84.649 16.361 52.785 1.00 68.68 B ATOM 2736 ND2 ASN B 476 86.668 17.167 53.405 1.00 65.78 B ATOM 2737 C ASN B 476 85.593 12.676 54.843 1.00 60.30 B ATOM 2738 O ASN B 476 85.828 12.036 53.822 1.00 61.52 B ATOM 2739 N ILE B 477 85.379 12.095 56.018 1.00 58.81 B ATOM 2740 CA ILE B 477 85.395 10.642 56.155 1.00 57.40 B ATOM 2741 CB ILE B 477 86.720 10.148 56.780 1.00 58.27 B ATOM 2742 CG2 ILE B 477 86.741 8.618 56.804 1.00 58.03 B ATOM 2743 CG1 ILE B 477 87.903 10.659 55.960 0.00 58.14 B ATOM 2744 CD1 ILE B 477 89.253 10.422 56.599 0.00 58.25 B ATOM 2745 C ILE B 477 84.224 10.183 57.030 1.00 55.59 B ATOM 2746 O ILE B 477 84.050 10.661 58.151 1.00 55.65 B ATOM 2747 N LYS B 478 83.423 9.257 56.515 1.00 52.92 B ATOM 2748 CA LYS B 478 82.281 8.760 57.264 1.00 51.69 B ATOM 2749 CB LYS B 478 81.106 8.479 56.322 1.00 50.04 B ATOM 2750 CG LYS B 478 80.324 9.717 55.899 1.00 47.12 B ATOM 2751 CD LYS B 478 78.972 9.329 55.324 1.00 46.70 B ATOM 2752 CE LYS B 478 78.106 10.553 55.048 1.00 45.79 B ATOM 2753 NZ LYS B 478 76.681 10.181 54.803 1.00 44.56 B ATOM 2754 C LYS B 478 82.591 7.509 58.090 1.00 52.07 B ATOM 2755 O LYS B 478 83.279 6.593 57.620 1.00 53.19 B ATOM 2756 N TYR B 479 82.076 7.485 59.323 1.00 51.09 B ATOM 2757 CA TYR B 479 82.273 6.363 60.250 1.00 49.59 B ATOM 2758 CB TYR B 479 83.083 6.815 61.492 1.00 50.00 B ATOM 2759 CG TYR B 479 84.438 7.442 61.183 1.00 49.78 B ATOM 2760 CD1 TYR B 479 84.526 8.594 60.402 1.00 50.71 B ATOM 2761 CE1 TYR B 479 85.754 9.165 60.062 1.00 49.52 B ATOM 2762 CD2 TYR B 479 85.629 6.869 61.630 1.00 49.70 B ATOM 2763 CE2 TYR B 479 86.870 7.438 61.291 1.00 49.93 B ATOM 2764 CZ TYR B 479 86.918 8.586 60.502 1.00 49.57 B ATOM 2765 OH TYR B 479 88.115 9.155 60.126 1.00 48.42 B ATOM 2766 C TYR B 479 80.922 5.790 60.698 1.00 48.39 B ATOM 2767 O TYR B 479 79.877 6.381 60.463 1.00 47.95 B ATOM 2768 N ILE B 480 80.954 4.629 61.337 1.00 48.14 B ATOM 2769 CA ILE B 480 79.742 3.986 61.828 1.00 47.98 B ATOM 2770 CB ILE B 480 79.470 2.669 61.090 1.00 47.82 B ATOM 2771 CG2 ILE B 480 78.250 1.983 61.679 1.00 48.23 B ATOM 2772 CG1 ILE B 480 79.275 2.929 59.599 1.00 47.92 B ATOM 2773 CD1 ILE B 480 79.279 1.675 58.768 1.00 46.66 B ATOM 2774 C ILE B 480 79.930 3.651 63.308 1.00 48.77 B ATOM 2775 O ILE B 480 80.961 3.089 63.699 1.00 49.54 B ATOM 2776 N VAL B 481 78.931 3.982 64.124 1.00 48.38 B ATOM 2777 CA VAL B 481 78.975 3.718 65.566 1.00 46.50 B ATOM 2778 CB VAL B 481 78.917 5.041 66.382 1.00 46.27 B ATOM 2779 CG1 VAL B 481 79.048 4.749 67.871 1.00 44.39 B ATOM 2780 CG2 VAL B 481 80.004 5.990 65.914 1.00 45.50 B ATOM 2781 C VAL B 481 77.778 2.855 65.962 1.00 45.57 B ATOM 2782 O VAL B 481 76.634 3.281 65.823 1.00 45.94 B ATOM 2783 N THR B 482 78.039 1.652 66.460 1.00 43.78 B ATOM 2784 CA THR B 482 76.963 0.752 66.865 1.00 43.35 B ATOM 2785 CB THR B 482 77.050 −0.608 66.091 1.00 44.57 B ATOM 2786 OG1 THR B 482 78.422 −0.943 65.851 1.00 44.68 B ATOM 2787 CG2 THR B 482 76.315 −0.523 64.748 1.00 44.18 B ATOM 2788 C THR B 482 76.946 0.475 68.379 1.00 42.32 B ATOM 2789 O THR B 482 77.979 0.184 68.977 1.00 42.34 B ATOM 2790 N GLY B 483 75.769 0.583 68.991 1.00 41.18 B ATOM 2791 CA GLY B 483 75.643 0.319 70.410 1.00 42.21 B ATOM 2792 C GLY B 483 75.021 −1.057 70.556 1.00 43.25 B ATOM 2793 O GLY B 483 74.069 −1.385 69.837 1.00 44.15 B ATOM 2794 N SER B 484 75.536 −1.865 71.479 1.00 42.55 B ATOM 2795 CA SER B 484 75.018 −3.216 71.650 1.00 42.61 B ATOM 2796 CB SER B 484 76.015 −4.236 71.071 1.00 42.00 B ATOM 2797 OG SER B 484 75.676 −5.572 71.425 1.00 39.48 B ATOM 2798 C SER B 484 74.721 −3.560 73.099 1.00 43.04 B ATOM 2799 O SER B 484 75.118 −2.833 74.007 1.00 43.14 B ATOM 2800 N ARG B 485 73.993 −4.664 73.294 1.00 43.38 B ATOM 2801 CA ARG B 485 73.628 −5.182 74.618 1.00 42.66 B ATOM 2802 CB ARG B 485 72.532 −6.233 74.484 1.00 41.35 B ATOM 2803 CG ARG B 485 71.309 −5.751 73.737 1.00 41.63 B ATOM 2804 CD ARG B 485 70.170 −5.535 74.696 1.00 40.30 B ATOM 2805 NE ARG B 485 69.101 −6.499 74.462 1.00 41.39 B ATOM 2806 CZ ARG B 485 67.859 −6.154 74.146 1.00 42.42 B ATOM 2807 NH1 ARG B 485 67.547 −4.874 74.029 1.00 44.59 B ATOM 2808 NH2 ARG B 485 66.927 −7.076 73.964 1.00 41.56 B ATOM 2809 C ARG B 485 74.879 −5.837 75.200 1.00 43.12 B ATOM 2810 O ARG B 485 74.845 −6.448 76.264 1.00 42.36 B ATOM 2811 N ASP B 486 75.974 −5.714 74.463 1.00 43.89 B ATOM 2812 CA ASP B 486 77.232 −6.263 74.880 1.00 44.86 B ATOM 2813 CB ASP B 486 78.100 −6.572 73.646 1.00 45.64 B ATOM 2814 CG ASP B 486 78.713 −5.327 73.012 1.00 46.63 B ATOM 2815 OD1 ASP B 486 78.016 −4.298 72.888 1.00 46.93 B ATOM 2816 OD2 ASP B 486 79.897 −5.387 72.619 1.00 47.67 B ATOM 2817 C ASP B 486 77.887 −5.242 75.807 1.00 45.67 B ATOM 2818 O ASP B 486 78.967 −5.486 76.344 1.00 46.05 B ATOM 2819 N ASN B 487 77.207 −4.108 76.003 1.00 45.49 B ATOM 2820 CA ASN B 487 77.673 −3.017 76.873 1.00 44.88 B ATOM 2821 CB ASN B 487 78.223 −3.571 78.188 1.00 44.56 B ATOM 2822 CG ASN B 487 77.171 −4.261 79.021 1.00 45.76 B ATOM 2823 OD1 ASN B 487 76.153 −4.717 78.508 1.00 47.63 B ATOM 2824 ND2 ASN B 487 77.421 −4.359 80.317 1.00 45.91 B ATOM 2825 C ASN B 487 78.748 −2.146 76.242 1.00 44.09 B ATOM 2826 O ASN B 487 79.333 −1.306 76.920 1.00 43.58 B ATOM 2827 N THR B 488 79.009 −2.347 74.953 1.00 44.03 B ATOM 2828 CA THR B 488 80.038 −1.576 74.267 1.00 45.88 B ATOM 2829 CB THR B 488 81.264 −2.458 73.895 1.00 46.72 B ATOM 2830 OG1 THR B 488 81.026 −3.098 72.633 1.00 46.03 B ATOM 2831 CG2 THR B 488 81.498 −3.545 74.958 1.00 47.35 B ATOM 2832 C THR B 488 79.525 −0.958 72.971 1.00 46.36 B ATOM 2833 O THR B 488 78.403 −1.224 72.542 1.00 47.28 B ATOM 2834 N LEU B 489 80.369 −0.135 72.355 1.00 45.88 B ATOM 2835 CA LEU B 489 80.053 0.511 71.090 1.00 46.03 B ATOM 2836 CB LEU B 489 79.848 2.015 71.269 1.00 45.02 B ATOM 2837 CG LEU B 489 78.651 2.443 72.110 1.00 44.47 B ATOM 2838 CD1 LEU B 489 79.093 2.732 73.518 1.00 43.21 B ATOM 2839 CD2 LEU B 489 78.011 3.655 71.484 1.00 45.05 B ATOM 2840 C LEU B 489 81.186 0.293 70.102 1.00 47.37 B ATOM 2841 O LEU B 489 82.281 0.840 70.280 1.00 48.75 B ATOM 2842 N HIS B 490 80.930 −0.507 69.067 1.00 46.28 B ATOM 2843 CA HIS B 490 81.940 −0.766 68.040 1.00 44.43 B ATOM 2844 CB HIS B 490 81.680 −2.105 67.363 1.00 46.31 B ATOM 2845 CG HIS B 490 81.979 −3.288 68.226 1.00 48.42 B ATOM 2846 CD2 HIS B 490 82.601 −4.456 67.944 1.00 48.94 B ATOM 2847 ND1 HIS B 490 81.584 −3.371 69.544 1.00 48.72 B ATOM 2848 CE1 HIS B 490 81.947 −4.542 70.035 1.00 48.74 B ATOM 2849 NE2 HIS B 490 82.566 −5.220 69.084 1.00 49.32 B ATOM 2850 C HIS B 490 81.932 0.332 66.988 1.00 41.63 B ATOM 2851 O HIS B 490 80.873 0.804 66.598 1.00 39.88 B ATOM 2852 N VAL B 491 83.119 0.727 66.537 1.00 41.79 B ATOM 2853 CA VAL B 491 83.268 1.774 65.523 1.00 43.45 B ATOM 2854 CB VAL B 491 84.258 2.873 65.987 1.00 43.37 B ATOM 2855 CG1 VAL B 491 84.565 3.838 64.843 1.00 43.14 B ATOM 2856 CG2 VAL B 491 83.661 3.642 67.158 1.00 42.84 B ATOM 2857 C VAL B 491 83.773 1.199 64.201 1.00 43.94 B ATOM 2858 O VAL B 491 84.794 0.515 64.165 1.00 45.06 B ATOM 2859 N TRP B 492 83.056 1.479 63.115 1.00 44.26 B ATOM 2860 CA TRP B 492 83.453 0.982 61.804 1.00 43.81 B ATOM 2861 CB TRP B 492 82.481 −0.086 61.312 1.00 42.52 B ATOM 2862 CG TRP B 492 81.869 −0.922 62.399 1.00 42.97 B ATOM 2863 CD2 TRP B 492 82.119 −2.308 62.661 1.00 43.02 B ATOM 2864 CE2 TRP B 492 81.258 −2.696 63.721 1.00 42.64 B ATOM 2865 CE3 TRP B 492 82.980 −3.262 62.102 1.00 42.84 B ATOM 2866 CD1 TRP B 492 80.906 −0.535 63.289 1.00 42.27 B ATOM 2867 NE1 TRP B 492 80.532 −1.593 64.081 1.00 42.22 B ATOM 2868 CZ2 TRP B 492 81.231 −4.000 64.235 1.00 43.33 B ATOM 2869 CZ3 TRP B 492 82.955 −4.562 62.613 1.00 43.23 B ATOM 2870 CR2 TRP B 492 82.083 −4.917 63.670 1.00 43.67 B ATOM 2871 C TRP B 492 83.493 2.123 60.804 1.00 44.22 B ATOM 2872 O TRP B 492 83.061 3.233 61.094 1.00 43.90 B ATOM 2873 N LYS B 493 84.033 1.847 59.627 1.00 45.31 B ATOM 2874 CA LYS B 493 84.115 2.855 58.596 1.00 46.28 B ATOM 2875 CB LYS B 493 85.515 2.896 57.997 1.00 47.20 B ATOM 2876 CG LYS B 493 86.600 3.104 59.021 1.00 48.93 B ATOM 2877 CD LYS B 493 87.962 3.179 58.363 0.00 48.94 B ATOM 2878 CE LYS B 493 89.061 3.374 59.394 0.00 49.30 B ATOM 2879 NZ LYS B 493 90.390 3.550 58.746 0.00 49.52 B ATOM 2880 C LYS B 493 83.108 2.522 57.518 1.00 47.32 B ATOM 2881 O LYS B 493 82.863 1.349 57.220 1.00 47.63 B ATOM 2882 N LEU B 494 82.514 3.563 56.952 1.00 47.99 B ATOM 2883 CA LEU B 494 81.539 3.395 55.895 1.00 48.33 B ATOM 2884 CB LEU B 494 80.733 4.674 55.717 1.00 48.56 B ATOM 2885 CG LEU B 494 79.698 4.594 54.604 1.00 48.11 B ATOM 2886 CD1 LEU B 494 78.587 3.650 55.032 1.00 47.88 B ATOM 2887 CD2 LEU B 494 79.156 5.988 54.313 1.00 49.20 B ATOM 2888 C LEU B 494 82.298 3.086 54.618 1.00 48.60 B ATOM 2889 O LEU B 494 83.009 3.938 54.096 1.00 48.84 B ATOM 2890 N PRO B 495 82.170 1.856 54.109 1.00 48.59 B ATOM 2891 CD PRO B 495 81.485 0.713 54.729 1.00 48.94 B ATOM 2892 CA PRO B 495 82.850 1.438 52.887 1.00 50.38 B ATOM 2893 CB PRO B 495 82.345 0.014 52.693 1.00 49.35 B ATOM 2894 CG PRO B 495 82.201 −0.461 54.107 1.00 48.48 B ATOM 2895 C PRO B 495 82.561 2.342 51.693 1.00 52.37 B ATOM 2896 O PRO B 495 81.415 2.741 51.456 1.00 53.23 B ATOM 2897 N LYS B 496 83.625 2.669 50.963 1.00 53.80 B ATOM 2898 CA LYS B 496 83.557 3.519 49.784 1.00 54.63 B ATOM 2899 CB LYS B 496 84.934 4.155 49.529 1.00 55.28 B ATOM 2900 CG LYS B 496 86.118 3.196 49.670 1.00 54.90 B ATOM 2901 CD LYS B 496 87.443 3.945 49.624 1.00 54.86 B ATOM 2902 CE LYS B 496 88.625 3.017 49.840 0.00 55.42 B ATOM 2903 NZ LYS B 496 89.917 3.759 49.828 0.00 55.70 B ATOM 2904 C LYS B 496 83.100 2.731 48.559 1.00 54.70 B ATOM 2905 O LYS B 496 82.693 3.317 47.553 1.00 54.41 B ATOM 2906 N ASP B 508 80.076 −10.950 44.143 1.00 87.67 B ATOM 2907 CA ASP B 508 81.314 −10.630 44.843 1.00 87.56 B ATOM 2908 CB ASP B 508 82.398 −10.224 43.855 1.00 85.57 B ATOM 2909 CG ASP B 508 82.370 −8.742 43.565 1.00 84.40 B ATOM 2910 OD1 ASP B 508 81.334 −8.260 43.072 1.00 83.24 B ATOM 2911 OD2 ASP B 508 83.371 −8.056 43.855 1.00 83.59 B ATOM 2912 C ASP B 508 81.080 −9.451 45.781 1.00 88.88 B ATOM 2913 O ASP B 508 82.036 −8.810 46.225 1.00 89.19 B ATOM 2914 N TYR B 509 79.812 −9.155 46.066 1.00 89.80 B ATOM 2915 CA TYR B 509 79.455 −8.033 46.939 1.00 89.61 B ATOM 2916 CB TYR B 509 78.210 −7.309 46.397 1.00 90.86 B ATOM 2917 CG TYR B 509 78.488 −5.981 45.705 1.00 92.99 B ATOM 2918 CD1 TYR B 509 77.576 −5.455 44.774 1.00 94.09 B ATOM 2919 CE1 TYR B 509 77.817 −4.236 44.120 1.00 94.93 B ATOM 2920 CD2 TYR B 509 79.653 −5.252 45.974 1.00 93.03 B ATOM 2921 CE2 TYR B 509 79.906 −4.032 45.329 1.00 94.38 B ATOM 2922 CZ TYR B 509 78.986 −3.530 44.401 1.00 95.32 B ATOM 2923 OH TYR B 509 79.241 −2.342 43.743 1.00 95.61 B ATOM 2924 C TYR B 509 79.236 −8.425 48.404 1.00 88.37 B ATOM 2925 O TYR B 509 79.772 −7.770 49.301 1.00 89.80 B ATOM 2926 N PRO B 510 78.448 −9.487 48.672 1.00 86.15 B ATOM 2927 CD PRO B 510 77.598 −10.261 47.751 1.00 84.82 B ATOM 2928 CA PRO B 510 78.214 −9.897 50.067 1.00 83.98 B ATOM 2929 CB PRO B 510 77.276 −11.093 49.923 1.00 84.08 B ATOM 2930 CG PRO B 510 76.518 −10.763 48.676 1.00 84.98 B ATOM 2931 C PRO B 510 79.508 −10.265 50.800 1.00 81.81 B ATOM 2932 O PRO B 510 79.788 −11.441 51.017 1.00 81.76 B ATOM 2933 N LEU B 511 80.289 −9.254 51.176 1.00 79.52 B ATOM 2934 CA LEU B 511 81.556 −9.462 51.875 1.00 77.45 B ATOM 2935 CB LEU B 511 82.466 −8.246 51.701 1.00 75.86 B ATOM 2936 CG LEU B 511 82.803 −7.866 50.264 1.00 74.15 B ATOM 2937 CD1 LEU B 511 83.709 −6.653 50.229 1.00 72.84 B ATOM 2938 CD2 LEU B 511 83.463 −9.053 49.601 1.00 74.63 B ATOM 2939 C LEU B 511 81.323 −9.689 53.355 1.00 77.25 B ATOM 2940 O LEU B 511 80.682 −8.878 54.020 1.00 77.95 B ATOM 2941 N VAL B 512 81.856 −10.785 53.877 1.00 76.40 B ATOM 2942 CA VAL B 512 81.683 −11.100 55.286 1.00 75.66 B ATOM 2943 CB VAL B 512 81.075 −12.495 55.458 1.00 74.68 B ATOM 2944 CG1 VAL B 512 80.748 −12.736 56.917 1.00 73.65 B ATOM 2945 CG2 VAL B 512 79.843 −12.625 54.587 1.00 73.90 B ATOM 2946 C VAL B 512 83.009 −11.040 56.029 1.00 75.90 B ATOM 2947 O VAL B 512 84.015 −11.558 55.560 1.00 76.65 B ATOM 2948 N PHE B 513 83.007 −10.394 57.187 1.00 75.87 B ATOM 2949 CA PHE B 513 84.218 −10.275 57.986 1.00 75.67 B ATOM 2950 CB PHE B 513 84.669 −8.820 58.058 1.00 74.40 B ATOM 2951 CG PHE B 513 84.758 −8.148 56.722 1.00 74.06 B ATOM 2952 CD1 PHE B 513 83.611 −7.885 55.981 1.00 74.40 B ATOM 2953 CD2 PHE B 513 85.987 −7.765 56.208 1.00 74.00 B ATOM 2954 CE1 PHE B 513 83.686 −7.246 54.752 1.00 74.32 B ATOM 2955 CE2 PHE B 513 86.077 −7.126 54.979 1.00 73.93 B ATOM 2956 CZ PHE B 513 84.921 −6.865 54.249 1.00 74.51 B ATOM 2957 C PHE B 513 83.893 −10.780 59.378 1.00 76.17 B ATOM 2958 O PHE B 513 83.367 −10.041 60.207 1.00 76.66 B ATOM 2959 N HIS B 514 84.203 −12.043 59.631 1.00 76.08 B ATOM 2960 CA HIS B 514 83.906 −12.636 60.919 1.00 76.38 B ATOM 2961 CB HIS B 514 83.697 −14.139 60.758 1.00 78.44 B ATOM 2962 CG HIS B 514 84.803 −14.820 60.022 1.00 81.60 B ATOM 2963 CD2 HIS B 514 85.579 −15.876 60.360 1.00 82.68 B ATOM 2964 ND1 HIS B 514 85.232 −14.407 58.780 1.00 82.91 B ATOM 2965 CE1 HIS B 514 86.228 −15.180 58.384 1.00 84.06 B ATOM 2966 NE2 HIS B 514 86.458 −16.079 59.324 1.00 83.92 B ATOM 2967 C HIS B 514 84.981 −12.355 61.948 1.00 75.65 B ATOM 2968 O HIS B 514 84.997 −12.964 63.016 1.00 75.17 B ATOM 2969 N THR B 515 85.880 −11.431 61.632 1.00 75.12 B ATOM 2970 CA THR B 515 86.931 −11.076 62.573 1.00 75.68 B ATOM 2971 CB THR B 515 88.219 −11.871 62.315 1.00 75.87 B ATOM 2972 OG1 THR B 515 87.936 −13.276 62.363 1.00 75.87 B ATOM 2973 CG2 THR B 515 89.255 −11.538 63.375 1.00 74.95 B ATOM 2974 C THR B 515 87.245 −9.590 62.492 1.00 75.55 B ATOM 2975 O THR B 515 87.642 −9.087 61.445 1.00 75.60 B ATOM 2976 N PRO B 516 87.061 −8.869 63.606 1.00 75.61 B ATOM 2977 CD PRO B 516 86.520 −9.405 64.867 1.00 76.30 B ATOM 2978 CA PRO B 516 87.308 −7.430 63.722 1.00 75.87 B ATOM 2979 CB PRO B 516 87.056 −7.161 65.202 1.00 76.07 B ATOM 2980 CG PRO B 516 86.008 −8.162 65.550 1.00 76.54 B ATOM 2981 C PRO B 516 88.719 −7.025 63.299 1.00 76.37 B ATOM 2982 O PRO B 516 88.897 −6.183 62.415 1.00 75.84 B ATOM 2983 N GLU B 517 89.714 −7.626 63.949 1.00 76.93 B ATOM 2984 CA GLU B 517 91.126 −7.356 63.676 1.00 76.76 B ATOM 2985 CB GLU B 517 91.996 −8.320 64.492 1.00 78.63 B ATOM 2986 CG GLU B 517 93.496 −8.083 64.384 1.00 81.28 B ATOM 2987 CD GLU B 517 93.944 −6.839 65.123 1.00 82.27 B ATOM 2988 OE1 GLU B 517 95.171 −6.593 65.192 1.00 83.01 B ATOM 2989 OE2 GLU B 517 93.066 −6.107 65.630 1.00 82.62 B ATOM 2990 C GLU B 517 91.448 −7.505 62.189 1.00 75.46 B ATOM 2991 O GLU B 517 92.318 −6.812 61.663 1.00 75.08 B ATOM 2992 N GLU B 518 90.733 −8.411 61.525 1.00 73.54 B ATOM 2993 CA GLU B 518 90.927 −8.681 60.106 1.00 71.48 B ATOM 2994 CB GLU B 518 90.530 −10.124 59.793 0.00 72.44 B ATOM 2995 CG GLU B 518 90.797 −10.526 58.359 0.00 73.10 B ATOM 2996 CD GLU B 518 90.441 −11.970 58.079 0.00 73.51 B ATOM 2997 OE1 GLU B 518 89.258 −12.335 58.243 0.00 73.72 B ATOM 2998 OE2 GLU B 518 91.346 −12.741 57.695 0.00 73.72 B ATOM 2999 C GLU B 518 90.145 −7.730 59.199 1.00 70.28 B ATOM 3000 O GLU B 518 90.596 −7.400 58.098 1.00 69.72 B ATOM 3001 N ASN B 519 88.977 −7.296 59.676 1.00 68.04 B ATOM 3002 CA ASN B 519 88.087 −6.380 58.947 1.00 65.05 B ATOM 3003 CB ASN B 519 86.773 −6.224 59.718 1.00 63.79 B ATOM 3004 CG ASN B 519 85.805 −5.267 59.053 1.00 62.26 B ATOM 3005 OD1 ASN B 519 84.702 −5.066 59.548 1.00 62.79 B ATOM 3006 ND2 ASN B 519 86.204 −4.676 57.933 1.00 60.05 B ATOM 3007 C ASN B 519 88.716 −5.000 58.728 1.00 63.93 B ATOM 3008 O ASN B 519 88.842 −4.220 59.669 1.00 64.23 B ATOM 3009 N PRO B 520 89.090 −4.673 57.473 1.00 62.40 B ATOM 3010 CD PRO B 520 88.866 −5.499 56.274 1.00 61.90 B ATOM 3011 CA PRO B 520 89.711 −3.396 57.096 1.00 60.68 B ATOM 3012 CB PRO B 520 89.820 −3.497 55.577 1.00 60.59 B ATOM 3013 CG PRO B 520 89.895 −4.957 55.331 1.00 61.94 B ATOM 3014 C PRO B 520 88.906 −2.174 57.500 1.00 60.35 B ATOM 3015 O PRO B 520 89.403 −1.049 57.445 1.00 60.91 B ATOM 3016 N TYR B 521 87.657 −2.399 57.888 1.00 58.53 B ATOM 3017 CA TYR B 521 86.774 −1.314 58.276 1.00 56.62 B ATOM 3018 CB TYR B 521 85.410 −1.538 57.636 1.00 56.52 B ATOM 3019 CG TYR B 521 85.470 −1.631 56.133 1.00 55.43 B ATOM 3020 CD1 TYR B 521 85.625 −0.493 55.356 1.00 53.35 B ATOM 3021 CE1 TYR B 521 85.684 −0.568 53.980 1.00 52.25 B ATOM 3022 CD2 TYR B 521 85.378 −2.860 55.487 1.00 55.47 B ATOM 3023 CE2 TYR B 521 85.437 −2.946 54.109 1.00 54.04 B ATOM 3024 CZ TYR B 521 85.587 −1.792 53.360 1.00 53.20 B ATOM 3025 OH TYR B 521 85.611 −1.862 51.986 1.00 53.19 B ATOM 3026 C TYR B 521 86.618 −1.168 59.782 1.00 56.07 B ATOM 3027 O TYR B 521 86.225 −0.109 60.264 1.00 55.68 B ATOM 3028 N PHE B 522 86.929 −2.227 60.521 1.00 55.73 B ATOM 3029 CA PHE B 522 86.797 −2.207 61.969 1.00 55.79 B ATOM 3030 CB PHE B 522 86.993 −3.605 62.543 1.00 57.01 B ATOM 3031 CG PHE B 522 86.935 −3.654 64.046 1.00 59.45 B ATOM 3032 CD1 PHE B 522 85.730 −3.458 64.719 1.00 60.43 B ATOM 3033 CD2 PHE B 522 88.084 −3.895 64.794 1.00 59.23 B ATOM 3034 CE1 PHE B 522 85.672 −3.505 66.119 1.00 60.50 B ATOM 3035 CE2 PHE B 522 88.032 −3.943 66.192 1.00 59.21 B ATOM 3036 CZ PHE B 522 86.825 −3.749 66.856 1.00 58.74 B ATOM 3037 C PHE B 522 87.764 −1.267 62.668 1.00 55.79 B ATOM 3038 O PHE B 522 88.899 −1.643 62.962 1.00 56.44 B ATOM 3039 N VAL B 523 87.314 −0.048 62.951 1.00 56.06 B ATOM 3040 CA VAL B 523 88.155 0.924 63.650 1.00 55.15 B ATOM 3041 CB VAL B 523 87.445 2.271 63.817 1.00 53.14 B ATOM 3042 CG1 VAL B 523 88.324 3.223 64.601 1.00 51.48 B ATOM 3043 CG2 VAL B 523 87.113 2.844 62.460 1.00 53.68 B ATOM 3044 C VAL B 523 88.506 0.384 65.035 1.00 55.15 B ATOM 3045 O VAL B 523 89.675 0.140 65.331 1.00 55.89 B ATOM 3046 N GLY B 524 87.489 0.187 65.870 1.00 53.67 B ATOM 3047 CA GLY B 524 87.726 −0.325 67.205 1.00 52.15 B ATOM 3048 C GLY B 524 86.521 −0.286 68.127 1.00 50.48 B ATOM 3049 O GLY B 524 85.504 0.329 67.821 1.00 50.52 B ATOM 3050 N VAL B 525 86.643 −0.933 69.277 1.00 48.79 B ATOM 3051 CA VAL B 525 85.555 −0.975 70.232 1.00 48.07 B ATOM 3052 CB VAL B 525 85.354 −2.418 70.744 1.00 46.89 B ATOM 3053 CG1 VAL B 525 86.674 −3.138 70.750 1.00 45.99 B ATOM 3054 CG2 VAL B 525 84.732 −2.403 72.130 1.00 45.90 B ATOM 3055 C VAL B 525 85.800 −0.015 71.392 1.00 47.57 B ATOM 3056 O VAL B 525 86.938 0.175 71.805 1.00 46.79 B ATOM 3057 N LEU B 526 84.727 0.603 71.894 1.00 48.52 B ATOM 3058 CA LEU B 526 84.811 1.567 73.005 1.00 48.97 B ATOM 3059 CB LEU B 526 84.199 2.910 72.583 1.00 47.57 B ATOM 3060 CG LEU B 526 84.696 3.601 71.310 1.00 47.85 B ATOM 3061 CD1 LEU B 526 83.713 4.694 70.936 1.00 48.90 B ATOM 3062 CD2 LEU B 526 86.082 4.170 71.496 1.00 46.34 B ATOM 3063 C LEU B 526 84.078 1.047 74.257 1.00 49.07 B ATOM 3064 O LEU B 526 82.862 1.207 74.382 1.00 49.55 B ATOM 3065 N ARG B 527 84.820 0.425 75.174 1.00 48.77 B ATOM 3066 CA ARG B 527 84.239 −0.119 76.402 1.00 48.18 B ATOM 3067 CB ARG B 527 85.016 −1.349 76.877 1.00 47.43 B ATOM 3068 CG ARG B 527 84.725 −2.604 76.074 1.00 47.62 B ATOM 3069 CD ARG B 527 85.540 −3.794 76.557 1.00 45.88 B ATOM 3070 NE ARG B 527 86.528 −4.196 75.561 1.00 44.94 B ATOM 3071 CZ ARG B 527 86.259 −4.860 74.439 1.00 43.61 B ATOM 3072 NH1 ARG B 527 85.014 −5.218 74.152 1.00 41.64 B ATOM 3073 NH2 ARG B 527 87.246 −5.158 73.594 1.00 41.55 B ATOM 3074 C ARG B 527 84.214 0.907 77.515 1.00 47.73 B ATOM 3075 O ARG B 527 85.162 1.662 77.703 1.00 46.73 B ATOM 3076 N GLY B 528 83.120 0.929 78.259 1.00 48.05 B ATOM 3077 CA GLY B 528 83.013 1.888 79.338 1.00 49.61 B ATOM 3078 C GLY B 528 81.677 1.823 80.047 1.00 50.20 B ATOM 3079 O GLY B 528 81.510 2.397 81.120 1.00 50.44 B ATOM 3080 N HIS B 529 80.718 1.126 79.448 1.00 51.40 B ATOM 3081 CA HIS B 529 79.392 0.990 80.040 1.00 52.69 B ATOM 3082 CB HIS B 529 78.308 1.270 78.997 1.00 53.42 B ATOM 3083 CG HIS B 529 77.908 2.711 78.931 1.00 54.66 B ATOM 3084 CD2 HIS B 529 78.036 3.710 79.836 1.00 54.96 B ATOM 3085 ND1 HIS B 529 77.284 3.264 77.835 1.00 54.53 B ATOM 3086 CE1 HIS B 529 77.046 4.542 78.066 1.00 54.69 B ATOM 3087 NE2 HIS B 529 77.493 4.837 79.273 1.00 55.98 B ATOM 3088 C HIS B 529 79.174 −0.376 80.664 1.00 52.47 B ATOM 3089 O HIS B 529 79.576 −1.396 80.112 1.00 53.72 B ATOM 3090 N MSE B 530 78.531 −0.379 81.825 1.00 52.35 B ATOM 3091 CA MSE B 530 78.260 −1.603 82.568 1.00 51.79 B ATOM 3092 CB MSE B 530 78.325 −1.325 84.068 1.00 54.89 B ATOM 3093 CG MSE B 530 79.640 −0.727 84.520 1.00 59.05 B ATOM 3094 SE MSE B 530 81.160 −1.831 84.066 1.00 66.13 B ATOM 3095 CE MSE B 530 81.008 −3.077 85.560 1.00 62.20 B ATOM 3096 C MSE B 530 76.894 −2.153 82.241 1.00 50.13 B ATOM 3097 O MSE B 530 76.318 −2.887 83.036 1.00 49.11 B ATOM 3098 N ALA B 531 76.379 −1.800 81.070 1.00 49.94 B ATOM 3099 CA ALA B 531 75.055 −2.246 80.658 1.00 48.69 B ATOM 3100 CB ALA B 531 73.999 −1.553 81.498 1.00 48.43 B ATOM 3101 C ALA B 531 74.843 −1.928 79.189 1.00 47.77 B ATOM 3102 O ALA B 531 75.669 −1.256 78.566 1.00 48.05 B ATOM 3103 N SER B 532 73.731 −2.414 78.645 1.00 46.82 B. ATOM 3104 CA SER B 532 73.380 −2.196 77.242 1.00 45.70 B ATOM 3105 CB SER B 532 72.036 −2.855 76.921 1.00 45.79 B ATOM 3106 OG SER B 532 71.413 −2.223 75.811 1.00 44.70 B ATOM 3107 C SER B 532 73.306 −0.733 76.839 1.00 44.93 B ATOM 3108 O SER B 532 72.834 0.118 77.595 1.00 45.32 B ATOM 3109 N VAL B 533 73.775 −0.469 75.627 1.00 43.79 B ATOM 3110 CA VAL B 533 73.771 0.865 75.038 1.00 43.92 B ATOM 3111 CB VAL B 533 75.002 1.045 74.123 1.00 42.68 B ATOM 3112 CG1 VAL B 533 74.893 2.335 73.336 1.00 42.48 B ATOM 3113 CG2 VAL B 533 76.274 1.027 74.965 1.00 41.21 B ATOM 3114 C VAL B 533 72.480 1.013 74.215 1.00 43.88 B ATOM 3115 O VAL B 533 72.398 0.518 73.085 1.00 43.85 B ATOM 3116 N ARG B 534 71.479 1.689 74.787 1.00 42.61 B ATOM 3117 CA ARG B 534 70.174 1.867 74.136 1.00 40.98 B ATOM 3118 CB ARG B 534 69.074 2.081 75.177 1.00 41.23 B ATOM 3119 CG ARG B 534 67.896 1.146 75.017 1.00 42.21 B ATOM 3120 CD ARG B 534 66.586 1.862 74.752 1.00 43.49 B ATOM 3121 NE ARG B 534 66.301 2.077 73.331 1.00 45.72 B ATOM 3122 CZ ARG B 534 65.097 1.903 72.792 1.00 47.54 B ATOM 3123 NH1 ARG B 534 64.093 1.508 73.563 1.00 46.82 B ATOM 3124 NH2 ARG B 534 64.884 2.136 71.499 1.00 50.38 B ATOM 3125 C ARG B 534 70.104 3.015 73.162 1.00 39.36 B ATOM 3126 O ARG B 534 69.339 2.975 72.200 1.00 38.05 B ATOM 3127 N THR B 535 70.889 4.050 73.426 1.00 38.74 B ATOM 3128 CA THR B 535 70.869 5.217 72.566 1.00 38.25 B ATOM 3129 CB THR B 535 70.062 6.362 73.233 1.00 39.86 B ATOM 3130 OG1 THR B 535 70.130 7.534 72.411 1.00 42.15 B ATOM 3131 CG2 THR B 535 70.596 6.661 74.630 1.00 39.79 B ATOM 3132 C THR B 535 72.263 5.686 72.189 1.00 36.40 B ATOM 3133 O THR B 535 73.212 5.478 72.934 1.00 34.48 B ATOM 3134 N VAL B 536 72.369 6.300 71.013 1.00 36.97 B ATOM 3135 CA VAL B 536 73.637 6.798 70.482 1.00 38.48 B ATOM 3136 CB VAL B 536 74.365 5.725 69.663 1.00 39.79 B ATOM 3137 CG1 VAL B 536 75.570 6.344 68.958 1.00 39.98 B ATOM 3138 CG2 VAL B 536 74.807 4.588 70.561 1.00 42.70 B ATOM 3139 C VAL B 536 73.417 7.969 69.538 1.00 37.98 B ATOM 3140 O VAL B 536 72.705 7.836 68.544 1.00 39.94 B ATOM 3141 N SER B 537 74.037 9.105 69.832 1.00 36.75 B ATOM 3142 CA SER B 537 73.904 10.281 68.978 1.00 35.47 B ATOM 3143 CB SER B 537 72.974 11.296 69.646 1.00 36.17 B ATOM 3144 OG SER B 537 73.057 12.572 69.032 1.00 36.43 B ATOM 3145 C SER B 537 75.280 10.889 68.744 1.00 34.85 B ATOM 3146 O SER B 537 76.071 11.009 69.671 1.00 33.64 B ATOM 3147 N GLY B 538 75.575 11.258 67.507 1.00 34.65 B ATOM 3148 CA GLY B 538 76.875 11.836 67.243 1.00 37.80 B ATOM 3149 C GLY B 538 76.900 12.740 66.030 1.00 39.65 B ATOM 3150 O GLY B 538 75.937 12.783 65.270 1.00 39.10 B ATOM 3151 N HIS B 539 78.004 13.462 65.857 1.00 42.51 B ATOM 3152 CA HIS B 539 78.193 14.382 64.736 1.00 44.95 B ATOM 3153 CB HIS B 539 77.370 15.657 64.927 1.00 48.76 B ATOM 3154 CG HIS B 539 75.912 15.402 65.134 1.00 54.64 B ATOM 3155 CD2 HIS B 539 75.121 15.566 66.221 1.00 55.81 B ATOM 3156 ND1 HIS B 539 75.112 14.845 64.158 1.00 55.89 B ATOM 3157 CE1 HIS B 539 73.891 14.677 64.635 1.00 56.19 B ATOM 3158 NE2 HIS B 539 73.870 15.106 65.885 1.00 56.92 B ATOM 3159 C HIS B 539 79.665 14.753 64.709 1.00 45.08 B ATOM 3160 O HIS B 539 80.167 15.351 65.659 1.00 45.61 B ATOM 3161 N GLY B 540 80.357 14.409 63.627 1.00 44.60 B ATOM 3162 CA GLY B 540 81.773 14.727 63.538 1.00 44.51 B ATOM 3163 C GLY B 540 82.612 13.714 64.300 1.00 44.45 B ATOM 3164 O GLY B 540 82.356 12.519 64.188 1.00 44.43 B ATOM 3165 N ASN B 541 83.612 14.182 65.054 1.00 44.24 B ATOM 3166 CA ASN B 541 84.482 13.304 65.841 1.00 43.77 B ATOM 3167 CB ASN B 541 85.914 13.855 65.925 1.00 43.91 B ATOM 3168 CG ASN B 541 86.011 15.119 66.773 1.00 45.62 B ATOM 3169 OD1 ASN B 541 85.399 16.139 66.449 1.00 46.42 B ATOM 3170 ND2 ASN B 541 86.783 15.054 67.867 1.00 45.00 B ATOM 3171 C ASN B 541 83.949 13.134 67.257 1.00 43.38 B ATOM 3172 O ASN B 541 84.662 12.651 68.139 1.00 44.20 B ATOM 3173 N ILE B 542 82.697 13.530 67.475 1.00 41.65 B ATOM 3174 CA ILE B 542 82.067 13.418 68.789 1.00 40.51 B ATOM 3175 CB ILE B 542 81.681 14.821 69.350 1.00 41.10 B ATOM 3176 CG2 ILE B 542 81.158 14.690 70.779 1.00 39.51 B ATOM 3177 CG1 ILE B 542 82.893 15.753 69.325 1.00 39.00 B ATOM 3178 CD1 ILE B 542 84.043 15.278 70.192 1.00 38.09 B ATOM 3179 C ILE B 542 80.795 12.560 68.744 1.00 39.78 B ATOM 3180 O ILE B 542 79.939 12.740 67.870 1.00 38.52 B ATOM 3181 N VAL B 543 80.687 11.630 69.691 1.00 38.75 B ATOM 3182 CA VAL B 543 79.523 10.752 69.799 1.00 38.25 B ATOM 3183 CB VAL B 543 79.775 9.342 69.183 1.00 37.58 B ATOM 3184 CG1 VAL B 543 78.596 8.430 69.454 1.00 34.60 B ATOM 3185 CG2 VAL B 543 79.995 9.459 67.678 1.00 39.64 B ATOM 3186 C VAL B 543 79.198 10.573 71.270 1.00 37.91 B ATOM 3187 O VAL B 543 80.098 10.411 72.091 1.00 40.30 B ATOM 3188 N VAL B 544 77.913 10.602 71.605 1.00 35.82 B ATOM 3189 CA VAL B 544 77.490 10.435 72.985 1.00 32.38 B ATOM 3190 CB VAL B 544 76.637 11.600 73.437 1.00 31.34 B ATOM 3191 CG1 VAL B 544 76.364 11.471 74.913 1.00 31.93 B ATOM 3192 CG2 VAL B 544 77.321 12.904 73.104 1.00 30.92 B ATOM 3193 C VAL B 544 76.652 9.186 73.089 1.00 31.39 B ATOM 3194 O VAL B 544 75.764 8.976 72.279 1.00 32.39 B ATOM 3195 N SER B 545 76.913 8.359 74.089 1.00 31.37 B ATOM 3196 CA SER B 545 76.136 7.135 74.238 1.00 32.82 B ATOM 3197 CB SER B 545 77.067 5.911 74.166 1.00 33.04 B ATOM 3198 OG SER B 545 77.887 5.768 75.328 1.00 31.94 B ATOM 3199 C SER B 545 75.290 7.062 75.522 1.00 34.31 B ATOM 3200 O SER B 545 75.663 7.595 76.576 1.00 35.23 B ATOM 3201 N GLY B 546 74.157 6.373 75.421 1.00 35.10 B ATOM 3202 CA GLY B 546 73.271 6.209 76.558 1.00 35.16 B ATOM 3203 C GLY B 546 73.064 4.744 76.889 1.00 35.12 B ATOM 3204 O GLY B 546 72.627 3.952 76.048 1.00 36.06 B ATOM 3205 N SER B 547 73.370 4.377 78.122 1.00 34.92 B ATOM 3206 CA SER B 547 73.219 2.996 78.520 1.00 35.83 B ATOM 3207 CB SER B 547 74.542 2.450 79.054 1.00 36.42 B ATOM 3208 OG SER B 547 74.376 1.145 79.580 1.00 37.41 B ATOM 3209 C SER B 547 72.146 2.811 79.569 1.00 36.27 B ATOM 3210 O SER B 547 71.561 3.776 80.043 1.00 35.05 B ATOM 3211 N TYR B 548 71.881 1.555 79.908 1.00 38.32 B ATOM 3212 CA TYR B 548 70.890 1.227 80.916 1.00 40.30 B ATOM 3213 CB TYR B 548 70.288 −0.146 80.629 1.00 42.68 B ATOM 3214 CG TYR B 548 69.117 −0.134 79.670 1.00 45.80 B ATOM 3215 CD1 TYR B 548 68.593 1.068 79.174 1.00 47.24 B ATOM 3216 CE1 TYR B 548 67.472 1.074 78.345 1.00 47.96 B ATOM 3217 CD2 TYR B 548 68.494 −1.322 79.302 1.00 45.36 B ATOM 3218 CE2 TYR B 548 67.385 −1.325 78.481 1.00 46.33 B ATOM 3219 CZ TYR B 548 66.873 −0.135 78.008 1.00 47.54 B ATOM 3220 OH TYR B 548 65.744 −0.162 77.223 1.00 49.19 B ATOM 3221 C TYR B 548 71.550 1.228 82.289 1.00 40.55 B ATOM 3222 O TYR B 548 70.898 0.990 83.305 1.00 40.82 B ATOM 3223 N ASP B 549 72.852 1.496 82.315 1.00 40.33 B ATOM 3224 CA ASP B 549 73.574 1.523 83.572 1.00 40.21 B ATOM 3225 CB ASP B 549 75.053 1.177 83.352 1.00 38.64 B ATOM 3226 CG ASP B 549 75.813 2.287 82.659 1.00 39.21 B ATOM 3227 OD1 ASP B 549 75.195 3.348 82.399 1.00 39.42 B ATOM 3228 OD2 ASP B 549 77.025 2.106 82.389 1.00 35.60 B ATOM 3229 C ASP B 549 73.437 2.905 84.207 1.00 41.08 B ATOM 3230 O ASP B 549 74.180 3.251 85.125 1.00 41.91 B ATOM 3231 N ASN B 550 72.490 3.693 83.696 1.00 41.46 B ATOM 3232 CA ASN B 550 72.213 5.043 84.208 1.00 41.90 B ATOM 3233 CB ASN B 550 71.853 4.982 85.696 1.00 42.29 B ATOM 3234 CG ASN B 550 70.885 3.882 86.013 1.00 42.40 B ATOM 3235 OD1 ASN B 550 70.421 3.181 85.117 1.00 44.98 B ATOM 3236 ND2 ASN B 550 70.563 3.723 87.289 1.00 41.54 B ATOM 3237 C ASN B 550 73.430 5.944 84.049 1.00 41.35 B ATOM 3238 O ASN B 550 73.934 6.498 85.034 1.00 41.70 B ATOM 3239 N THR B 551 73.891 6.101 82.816 1.00 40.29 B ATOM 3240 CA THR B 551 75.081 6.890 82.562 1.00 40.46 B ATOM 3241 CB THR B 551 76.344 6.109 83.031 1.00 40.37 B ATOM 3242 OG1 THR B 551 76.524 6.278 84.437 1.00 40.39 B ATOM 3243 CG2 THR B 551 77.576 6.547 82.288 1.00 39.19 B ATOM 3244 C THR B 551 75.230 7.167 81.080 1.00 41.05 B ATOM 3245 O THR B 551 74.793 6.374 80.250 1.00 41.68 B ATOM 3246 N LEU B 552 75.849 8.295 80.754 1.00 40.71 B ATOM 3247 CA LEU B 552 76.098 8.659 79.368 1.00 40.16 B ATOM 3248 CB LEU B 552 75.354 9.943 78.994 1.00 39.03 B ATOM 3249 CG LEU B 552 73.828 9.882 78.968 1.00 38.53 B ATOM 3250 CD1 LEU B 552 73.257 10.693 80.130 1.00 38.23 B ATOM 3251 CD2 LEU B 552 73.327 10.416 77.631 1.00 37.33 B ATOM 3252 C LEU B 552 77.591 8.888 79.253 1.00 40.99 B ATOM 3253 O LEU B 552 78.225 9.325 80.213 1.00 41.44 B ATOM 3254 N ILE B 553 78.160 8.579 78.093 1.00 41.46 B ATOM 3255 CA ILE B 553 79.589 8.788 77.879 1.00 41.69 B ATOM 3256 CB ILE B 553 80.366 7.452 77.679 1.00 41.75 B ATOM 3257 CG2 ILE B 553 81.854 7.746 77.598 1.00 41.32 B ATOM 3258 CG1 ILE B 553 80.077 6.451 78.811 1.00 42.93 B ATOM 3259 CD1 ILE B 553 80.616 6.835 80.176 1.00 42.43 B ATOM 3260 C ILE B 553 79.774 9.615 76.612 1.00 41.85 B ATOM 3261 O ILE B 553 79.057 9.419 75.631 1.00 41.17 B ATOM 3262 N VAL B 554 80.724 10.547 76.638 1.00 42.67 B ATOM 3263 CA VAL B 554 81.022 11.371 75.467 1.00 43.83 B ATOM 3264 CB VAL B 554 81.216 12.850 75.832 1.00 43.23 B ATOM 3265 CG1 VAL B 554 81.219 13.690 74.566 1.00 41.99 B ATOM 3266 CG2 VAL B 554 80.143 13.294 76.799 1.00 43.78 B ATOM 3267 C VAL B 554 82.344 10.858 74.907 1.00 44.98 B ATOM 3268 O VAL B 554 83.391 11.108 75.489 1.00 45.12 B ATOM 3269 N TRP B 555 82.305 10.152 73.782 1.00 46.53 B ATOM 3270 CA TRP B 555 83.526 9.603 73.198 1.00 48.33 B ATOM 3271 CB TRP B 555 83.264 8.193 72.652 1.00 48.73 B ATOM 3272 CG TRP B 555 82.491 7.287 73.562 1.00 48.42 B ATOM 3273 CD2 TRP B 555 83.024 6.244 74.390 1.00 49.05 B ATOM 3274 CE2 TRP B 555 81.934 5.644 75.060 1.00 49.51 B ATOM 3275 CE3 TRP B 555 84.317 5.758 74.629 1.00 48.35 B ATOM 3276 CD1 TRP B 555 81.140 7.281 73.762 1.00 48.53 B ATOM 3277 NE1 TRP B 555 80.797 6.296 74.661 1.00 49.31 B ATOM 3278 CZ2 TRP B 555 82.099 4.579 75.958 1.00 49.91 B ATOM 3279 CZ3 TRP B 555 84.481 4.698 75.523 1.00 47.73 B ATOM 3280 CR2 TRP B 555 83.378 4.121 76.174 1.00 48.67 B ATOM 3281 C TRP B 555 84.119 10.455 72.074 1.00 49.09 B ATOM 3282 O TRP B 555 83.424 11.253 71.451 1.00 48.46 B ATOM 3283 N ASP B 556 85.411 10.265 71.816 1.00 51.15 B ATOM 3284 CA ASP B 556 86.119 10.978 70.745 1.00 52.97 B ATOM 3285 CB ASP B 556 87.358 11.705 71.295 1.00 53.47 B ATOM 3286 CG ASP B 556 88.047 12.594 70.247 1.00 53.63 B ATOM 3287 OD1 ASP B 556 88.097 12.203 69.060 1.00 52.44 B ATOM 3288 OD2 ASP B 556 88.552 13.683 70.615 1.00 53.83 B ATOM 3289 C ASP B 556 86.569 9.933 69.726 1.00 53.38 B ATOM 3290 O ASP B 556 87.740 9.560 69.688 1.00 54.18 B ATOM 3291 N VAL B 557 85.635 9.460 68.909 1.00 54.03 B ATOM 3292 CA VAL B 557 85.925 8.446 67.896 1.00 53.93 B ATOM 3293 CB VAL B 557 84.859 8.493 66.780 1.00 53.70 B ATOM 3294 CG1 VAL B 557 85.210 7.519 65.660 1.00 54.83 B ATOM 3295 CG2 VAL B 557 83.502 8.151 67.370 1.00 52.75 B ATOM 3296 C VAL B 557 87.327 8.578 67.295 1.00 54.01 B ATOM 3297 O VAL B 557 88.014 7.575 67.065 1.00 53.12 B ATOM 3298 N ALA B 558 87.752 9.817 67.063 1.00 54.57 B ATOM 3299 CA ALA B 558 89.071 10.087 66.497 1.00 55.27 B ATOM 3300 CB ALA B 558 89.249 11.577 66.286 1.00 54.44 B ATOM 3301 C ALA B 558 90.189 9.554 67.393 1.00 56.09 B ATOM 3302 O ALA B 558 91.154 8.948 66.917 1.00 57.14 B ATOM 3303 N GLN B 559 90.054 9.779 68.693 1.00 56.27 B ATOM 3304 CA GLN B 559 91.052 9.325 69.652 1.00 56.00 B ATOM 3305 CB GLN B 559 91.358 10.445 70.643 1.00 57.58 B ATOM 3306 CG GLN B 559 91.679 11.771 69.977 1.00 60.76 B ATOM 3307 CD GLN B 559 92.288 12.773 70.944 1.00 63.21 B ATOM 3308 OE1 GLN B 559 91.798 12.942 72.072 1.00 63.29 B ATOM 3309 NE2 GLN B 559 93.360 13.449 70.510 1.00 62.95 B ATOM 3310 C GLN B 559 90.556 8.090 70.400 1.00 54.82 B ATOM 3311 O CLN B 559 91.131 7.679 71.407 1.00 53.08 B ATOM 3312 N MSE B 560 89.486 7.500 69.885 1.00 54.44 B ATOM 3313 CA MSE B 560 88.881 6.322 70.487 1.00 54.74 B ATOM 3314 CB MSE B 560 89.450 5.055 69.844 1.00 54.65 B ATOM 3315 CG MSE B 560 89.124 4.912 68.360 1.00 54.73 B ATOM 3316 SE MSE B 560 87.225 4.845 67.991 1.00 57.83 B ATOM 3317 CE MSE B 560 86.882 2.985 68.379 1.00 53.96 B ATOM 3318 C MSE B 560 89.041 6.275 72.013 1.00 54.33 B ATOM 3319 O MSE B 560 89.330 5.230 72.600 1.00 54.09 B ATOM 3320 N LYS B 561 88.838 7.419 72.654 1.00 53.76 B ATOM 3321 CA LYS B 561 88.945 7.494 74.100 1.00 53.03 B ATOM 3322 CB LYS B 561 90.168 8.331 74.473 0.00 53.61 B ATOM 3323 CG LYS B 561 90.538 8.294 75.933 0.00 54.07 B ATOM 3324 CD LYS B 561 91.867 8.981 76.146 0.00 54.52 B ATOM 3325 CE LYS B 561 92.219 9.039 77.612 0.00 54.82 B ATOM 3326 NZ LYS B 561 91.225 9.852 78.361 0.00 55.11 B ATOM 3327 C LYS B 561 87.663 8.092 74.690 1.00 52.48 B ATOM 3328 O LYS B 561 86.786 8.548 73.952 1.00 53.43 B ATOM 3329 N CYS B 562 87.553 8.063 76.018 1.00 50.98 B ATOM 3330 CA CYS B 562 86.394 8.601 76.740 1.00 48.94 B ATOM 3331 CB CYS B 562 86.209 7.834 78.056 1.00 49.61 B ATOM 3332 SG CYS B 562 85.037 8.536 79.259 1.00 51.47 B ATOM 3333 C CYS B 562 86.646 10.076 77.029 1.00 47.64 B ATOM 3334 O CYS B 562 87.772 10.450 77.339 1.00 48.22 B ATOM 3335 N LEU B 563 85.616 10.915 76.909 1.00 46.12 B ATOM 3336 CA LEU B 563 85.771 12.346 77.175 1.00 44.98 B ATOM 3337 CB LEU B 563 85.149 13.187 76.051 1.00 44.96 B ATOM 3338 CG LEU B 563 85.894 13.179 74.706 1.00 46.73 B ATOM 3339 CD1 LEU B 563 85.234 14.142 73.721 1.00 45.90 B ATOM 3340 CD2 LEU B 563 87.346 13.583 74.931 1.00 45.81 B ATOM 3341 C LEU B 563 85.165 12.731 78.518 1.00 43.88 B ATOM 3342 O LEU B 563 85.823 13.367 79.348 1.00 43.62 B ATOM 3343 N TYR B 564 83.913 12.345 78.731 1.00 42.63 B ATOM 3344 CA TYR B 564 83.244 12.632 79.986 1.00 41.64 B ATOM 3345 CB TYR B 564 82.429 13.918 79.887 1.00 41.63 B ATOM 3346 CG TYR B 564 83.248 15.149 79.592 1.00 42.86 B ATOM 3347 CD1 TYR B 564 83.298 15.684 78.308 1.00 43.33 B ATOM 3348 CE1 TYR B 564 84.049 16.819 78.036 1.00 45.08 B ATOM 3349 CD2 TYR B 564 83.976 15.782 80.602 1.00 43.76 B ATOM 3350 CE2 TYR B 564 84.732 16.916 80.341 1.00 43.78 B ATOM 3351 CZ TYR B 564 84.760 17.426 79.060 1.00 46.05 B ATOM 3352 OH TYR B 564 85.492 18.558 78.795 1.00 48.58 B ATOM 3353 C TYR B 564 82.321 11.491 80.356 1.00 41.77 B ATOM 3354 O TYR B 564 81.899 10.722 79.489 1.00 42.27 B ATOM 3355 N ILE B 565 82.011 11.391 81.647 1.00 41.33 B ATOM 3356 CA ILE B 565 81.116 10.358 82.156 1.00 40.82 B ATOM 3357 CB ILE B 565 81.828 9.414 83.169 1.00 41.48 B ATOM 3358 CG2 ILE B 565 80.934 8.234 83.486 1.00 40.38 B ATOM 3359 CG1 ILE B 565 83.126 8.862 82.582 1.00 40.59 B ATOM 3360 CD1 ILE B 565 83.907 8.008 83.571 1.00 41.08 B ATOM 3361 C ILE B 565 79.938 11.020 82.860 1.00 40.09 B ATOM 3362 O ILE B 565 79.853 11.020 84.089 1.00 41.84 B ATOM 3363 N LEU B 566 79.033 11.582 82.067 1.00 38.80 B ATOM 3364 CA LEU B 566 77.841 12.256 82.580 1.00 36.98 B ATOM 3365 CB LEU B 566 76.990 12.754 81.421 1.00 36.01 B ATOM 3366 CG LEU B 566 77.792 13.369 80.272 1.00 35.51 B ATOM 3367 CD1 LEU B 566 76.846 13.709 79.138 1.00 34.67 B ATOM 3368 CD2 LEU B 566 78.541 14.592 80.757 1.00 33.68 B ATOM 3369 C LEU B 566 77.010 11.306 83.411 1.00 36.96 B ATOM 3370 O LEU B 566 76.354 10.414 82.877 1.00 36.93 B ATOM 3371 N SER B 567 77.021 11.498 84.721 1.00 37.95 B ATOM 3372 CA SER B 567 76.252 10.628 85.601 1.00 39.30 B ATOM 3373 CB SER B 567 77.191 9.655 86.305 1.00 39.73 B ATOM 3374 OG SER B 567 78.238 10.359 86.940 1.00 40.54 B ATOM 3375 C SER B 567 75.466 11.417 86.635 1.00 39.56 B ATOM 3376 O SER B 567 76.007 12.260 87.344 1.00 39.82 B ATOM 3377 N GLY B 568 74.181 11.116 86.728 1.00 40.79 B ATOM 3378 CA GLY B 568 73.338 11.798 87.685 1.00 40.25 B ATOM 3379 C GLY B 568 71.949 11.190 87.704 1.00 40.41 B ATOM 3380 O GLY B 568 71.270 11.232 88.723 1.00 41.14 B ATOM 3381 N HIS B 569 71.513 10.636 86.575 1.00 40.65 B ATOM 3382 CA HIS B 569 70.197 10.017 86.508 1.00 40.96 B ATOM 3383 CB HIS B 569 69.865 9.568 85.077 1.00 40.33 B ATOM 3384 CG HIS B 569 69.511 10.695 84.151 1.00 40.43 B ATOM 3385 CD2 HIS B 569 68.558 11.657 84.232 1.00 39.98 B ATOM 3386 ND1 HIS B 569 70.194 10.936 82.977 1.00 40.06 B ATOM 3387 CE1 HIS B 569 69.681 11.995 82.378 1.00 38.53 B ATOM 3388 NE2 HIS B 569 68.687 12.452 83.118 1.00 38.90 B ATOM 3389 C HIS B 569 70.193 8.822 87.448 1.00 40.82 B ATOM 3390 O HIS B 569 71.239 8.242 87.743 1.00 39.68 B ATOM 3391 N THR B 570 69.007 8.464 87.915 1.00 41.28 B ATOM 3392 CA THR B 570 68.857 7.364 88.838 1.00 41.75 B ATOM 3393 CB THR B 570 68.025 7.806 90.042 1.00 42.58 B ATOM 3394 OG1 THR B 570 68.417 9.135 90.414 1.00 41.17 B ATOM 3395 CG2 THR B 570 68.265 6.872 91.226 1.00 44.09 B ATOM 3396 C THR B 570 68.201 6.169 88.168 1.00 41.63 B ATOM 3397 O THR B 570 67.554 5.348 88.824 1.00 42.87 B ATOM 3398 N ASP B 571 68.348 6.087 86.852 1.00 40.41 B ATOM 3399 CA ASP B 571 67.795 4.969 86.116 1.00 38.73 B ATOM 3400 CB ASP B 571 66.273 4.960 86.200 1.00 37.92 B ATOM 3401 CG ASP B 571 65.726 3.569 86.446 1.00 38.68 B ATOM 3402 OD1 ASP B 571 66.270 2.616 85.852 1.00 37.31 B ATOM 3403 OD2 ASP B 571 64.757 3.425 87.225 1.00 39.84 B ATOM 3404 C ASP B 571 68.240 4.941 84.663 1.00 38.21 B ATOM 3405 O ASP B 571 68.800 5.914 84.147 1.00 37.05 B ATOM 3406 N ARG B 572 67.994 3.806 84.016 1.00 38.06 B ATOM 3407 CA ARG B 572 68.365 3.602 82.620 1.00 38.61 B ATOM 3408 CB ARG B 572 67.761 2.282 82.102 1.00 39.79 B ATOM 3409 CG ARG B 572 66.409 1.944 82.735 1.00 42.08 B ATOM 3410 CD ARG B 572 65.669 0.771 82.066 1.00 43.20 B ATOM 3411 NE ARG B 572 66.402 −0.497 82.046 1.00 42.53 B ATOM 3412 CZ ARG B 572 65.859 −1.671 81.722 1.00 42.93 B ATOM 3413 NH1 ARG B 572 64.573 −1.757 81.395 1.00 41.39 B ATOM 3414 NH2 ARG B 572 66.605 −2.764 81.708 1.00 43.19 B ATOM 3415 C ARG B 572 67.961 4.764 81.712 1.00 37.29 B ATOM 3416 O ARG B 572 66.923 5.408 81.911 1.00 37.19 B ATOM 3417 N ILE B 573 68.803 5.022 80.716 1.00 34.87 B ATOM 3418 CA ILE B 573 68.589 6.088 79.739 1.00 32.30 B ATOM 3419 CB ILE B 573 69.914 6.783 79.417 1.00 31.72 B ATOM 3420 CG2 ILE B 573 69.736 7.751 78.276 1.00 29.59 B ATOM 3421 CG1 ILE B 573 70.434 7.465 80.678 1.00 33.36 B ATOM 3422 CD1 ILE B 573 71.875 7.918 80.574 1.00 34.32 B ATOM 3423 C ILE B 573 68.024 5.489 78.454 1.00 30.51 B ATOM 3424 O ILE B 573 68.467 4.441 78.009 1.00 29.57 B ATOM 3425 N TYR B 574 67.039 6.148 77.862 1.00 29.36 B ATOM 3426 CA TYR B 574 66.453 5.629 76.638 1.00 29.00 B ATOM 3427 CB TYR B 574 64.944 5.478 76.795 1.00 29.33 B ATOM 3428 CG TYR B 574 64.557 4.229 77.537 1.00 31.08 B ATOM 3429 CD1 TYR B 574 65.140 3.926 78.754 1.00 33.15 B ATOM 3430 CE1 TYR B 574 64.782 2.797 79.465 1.00 33.55 B ATOM 3431 CD2 TYR B 574 63.596 3.358 77.036 1.00 32.28 B ATOM 3432 CE2 TYR B 574 63.225 2.209 77.748 1.00 32.21 B ATOM 3433 CZ TYR B 574 63.828 1.947 78.970 1.00 32.73 B ATOM 3434 OH TYR B 574 63.457 0.871 79.743 1.00 34.36 B ATOM 3435 C TYR B 574 66.745 6.452 75.393 1.00 28.82 B ATOM 3436 O TYR B 574 66.611 5.965 74.264 1.00 28.32 B ATOM 3437 N SER B 575 67.169 7.692 75.590 1.00 28.07 B ATOM 3438 CA SER B 575 67.431 8.564 74.461 1.00 27.39 B ATOM 3439 CB SER B 575 66.101 9.147 73.980 1.00 27.09 B ATOM 3440 OC SER B 575 66.260 9.948 72.833 1.00 23.40 B ATOM 3441 C SER B 575 68.368 9.690 74.832 1.00 27.21 B ATOM 3442 O SER B 575 68.400 10.124 75.979 1.00 29.42 B ATOM 3443 N THR B 576 69.131 10.169 73.859 1.00 26.42 B ATOM 3444 CA THR B 576 70.036 11.279 74.101 1.00 24.44 B ATOM 3445 CB THR B 576 71.350 10.794 74.680 1.00 23.42 B ATOM 3446 OG1 THR B 576 72.176 11.925 74.958 1.00 22.28 B ATOM 3447 CG2 THR B 576 72.070 9.898 73.680 1.00 23.95 B ATOM 3448 C THR B 576 70.314 11.995 72.782 1.00 24.66 B ATOM 3449 O THR B 576 70.225 11.405 71.712 1.00 23.66 B ATOM 3450 N ILE B 577 70.639 13.274 72.843 1.00 25.19 B ATOM 3451 CA ILE B 577 70.938 13.979 71.615 1.00 24.85 B ATOM 3452 CB ILE B 577 69.767 14.869 71.172 1.00 23.89 B ATOM 3453 CG2 ILE B 577 70.271 15.939 70.202 1.00 21.80 B ATOM 3454 CG1 ILE B 577 68.671 14.011 70.538 1.00 23.81 B ATOM 3455 CD1 ILE B 577 67.376 14.750 70.224 1.00 21.31 B ATOM 3456 C ILE B 577 72.163 14.851 71.802 1.00 26.44 B ATOM 3457 O ILE B 577 72.324 15.497 72.833 1.00 26.92 B ATOM 3458 N TYR B 578 73.037 14.850 70.802 1.00 27.45 B ATOM 3459 CA TYR B 578 74.235 15.672 70.848 1.00 27.93 B ATOM 3460 CB TYR B 578 75.423 14.925 70.226 1.00 28.17 B ATOM 3461 CG TYR B 578 76.688 15.757 70.084 1.00 30.25 B ATOM 3462 CD1 TYR B 578 77.096 16.629 71.089 1.00 28.62 B ATOM 3463 CE1 TYR B 578 78.235 17.416 70.934 1.00 29.38 B ATOM 3464 CD2 TYR B 578 77.464 15.690 68.922 1.00 31.91 B ATOM 3465 CE2 TYR B 578 78.607 16.476 68.762 1.00 30.14 B ATOM 3466 CZ TYR B 578 78.980 17.334 69.767 1.00 29.57 B ATOM 3467 OH TYR B 578 80.082 18.135 69.605 1.00 31.32 B ATOM 3468 C TYR B 578 73.943 16.980 70.117 1.00 27.87 B ATOM 3469 O TYR B 578 73.789 17.017 68.897 1.00 27.54 B ATOM 3470 N ASP B 579 73.832 18.045 70.901 1.00 28.90 B ATOM 3471 CA ASP B 579 73.551 19.369 70.380 1.00 30.92 B ATOM 3472 CB ASP B 579 72.799 20.203 71.416 1.00 30.53 B ATOM 3473 CG ASP B 579 72.248 21.473 70.839 1.00 34.02 B ATOM 3474 OD1 ASP B 579 72.845 21.995 69.868 1.00 35.60 B ATOM 3475 OD2 ASP B 579 71.219 21.968 71.357 1.00 37.17 B ATOM 3476 C ASP B 579 74.871 20.026 70.035 1.00 31.94 B ATOM 3477 O ASP B 579 75.344 20.923 70.732 1.00 30.49 B ATOM 3478 N HIS B 580 75.461 19.557 68.945 1.00 34.88 B ATOM 3479 CA HIS B 580 76.731 20.085 68.492 1.00 38.67 B ATOM 3480 CB HIS B 580 77.133 19.422 67.170 1.00 40.80 B ATOM 3481 CG HIS B 580 76.123 19.579 66.080 1.00 44.94 B ATOM 3482 CD2 HIS B 580 76.268 19.900 64.773 1.00 46.55 B ATOM 3483 ND1 HIS B 580 74.778 19.359 66.276 1.00 47.64 B ATOM 3484 CE1 HIS B 580 74.135 19.532 65.132 1.00 47.95 B ATOM 3485 NE2 HIS B 580 75.016 19.860 64.206 1.00 46.75 B ATOM 3486 C HIS B 580 76.684 21.601 68.364 1.00 39.17 B ATOM 3487 O HIS B 580 77.545 22.297 68.907 1.00 40.61 B ATOM 3488 N GLU B 581 75.673 22.122 67.681 1.00 39.97 B ATOM 3489 CA GLU B 581 75.563 23.566 67.529 1.00 40.63 B ATOM 3490 CB GLU B 581 74.162 23.960 67.078 1.00 42.60 B ATOM 3491 CG GLU B 581 73.991 25.469 66.960 1.00 46.26 B ATOM 3492 CD GLU B 581 72.848 25.853 66.052 1.00 47.68 B ATOM 3493 OE1 GLU B 581 72.857 25.407 64.880 1.00 48.93 B ATOM 3494 OE2 GLU B 581 71.952 26.598 66.508 1.00 48.37 B ATOM 3495 C GLU B 581 75.871 24.279 68.836 1.00 40.05 B ATOM 3496 O GLU B 581 76.810 25.063 68.916 1.00 40.37 B ATOM 3497 N ARG B 582 75.074 23.998 69.859 1.00 39.74 B ATOM 3498 CA ARG B 582 75.266 24.622 71.151 1.00 38.74 B ATOM 3499 CB ARG B 582 73.939 24.647 71.899 1.00 37.10 B ATOM 3500 CG ARG B 582 73.131 25.905 71.619 1.00 37.06 B ATOM 3501 CD ARG B 582 71.654 25.749 71.970 1.00 35.83 B ATOM 3502 NE ARG B 582 70.962 24.890 71.012 1.00 35.08 B ATOM 3503 CZ ARG B 582 70.041 25.312 70.154 1.00 34.96 B ATOM 3504 NH1 ARG B 582 69.691 26.591 70.130 1.00 32.75 B ATOM 3505 NH2 ARG B 582 69.466 24.448 69.327 1.00 35.91 B ATOM 3506 C ARG B 582 76.356 23.971 71.989 1.00 39.71 B ATOM 3507 O ARG B 582 76.775 24.529 73.003 1.00 40.75 B ATOM 3508 N LYS B 583 76.825 22.804 71.548 1.00 40.22 B ATOM 3509 CA LYS B 583 77.881 22.056 72.240 1.00 39.65 B ATOM 3510 CB LYS B 583 79.089 22.961 72.487 1.00 41.30 B ATOM 3511 CG LYS B 583 80.401 22.212 72.649 1.00 43.06 B ATOM 3512 CD LYS B 583 80.866 21.664 71.311 1.00 46.02 B ATOM 3513 CE LYS B 583 81.196 22.806 70.367 1.00 46.16 B ATOM 3514 NZ LYS B 583 82.256 23.657 70.976 1.00 46.38 B ATOM 3515 C LYS B 583 77.357 21.524 73.574 1.00 38.48 B ATOM 3516 O LYS B 583 77.990 21.689 74.615 1.00 37.90 B ATOM 3517 N ARG B 584 76.202 20.871 73.526 1.00 36.80 B ATOM 3518 CA ARG B 584 75.575 20.343 74.728 1.00 36.72 B ATOM 3519 CB ARG B 584 74.436 21.278 75.140 1.00 35.58 B ATOM 3520 CG ARG B 584 74.930 22.481 75.916 1.00 38.40 B ATOM 3521 CD ARG B 584 74.542 23.820 75.330 1.00 37.40 B ATOM 3522 NE ARG B 584 73.160 24.166 75.635 1.00 39.31 B ATOM 3523 CZ ARG B 584 72.723 25.408 75.833 1.00 40.87 B ATOM 3524 NH1 ARG B 584 73.556 26.437 75.759 1.00 40.61 B ATOM 3525 NH2 ARG B 584 71.448 25.617 76.122 1.00 40.77 B ATOM 3526 C ARG B 584 75.045 18.915 74.573 1.00 36.65 B ATOM 3527 O ARG B 584 75.211 18.298 73.522 1.00 36.06 B ATOM 3528 N CYS B 585 74.443 18.372 75.631 1.00 36.04 B ATOM 3529 CA CYS B 585 73.847 17.043 75.534 1.00 34.78 B ATOM 3530 CB CYS B 585 74.778 15.936 75.994 1.00 36.01 B ATOM 3531 SG CYS B 585 73.955 14.322 75.938 1.00 38.57 B ATOM 3532 C CYS B 585 72.566 16.929 76.330 1.00 33.64 B ATOM 3533 O CYS B 585 72.503 17.328 77.495 1.00 33.83 B ATOM 3534 N ILE B 586 71.544 16.397 75.668 1.00 31.40 B ATOM 3535 CA ILE B 586 70.247 16.182 76.277 1.00 31.62 B ATOM 3536 CB ILE B 586 69.079 16.610 75.325 1.00 29.83 B ATOM 3537 CG2 ILE B 586 67.725 16.305 75.961 1.00 25.17 B ATOM 3538 CG1 ILE B 586 69.155 18.111 75.009 1.00 28.59 B ATOM 3539 CD1 ILE B 586 69.610 18.438 73.588 1.00 27.79 B ATOM 3540 C ILE B 586 70.135 14.680 76.534 1.00 33.85 B ATOM 3541 O ILE B 586 70.530 13.882 75.679 1.00 35.25 B ATOM 3542 N SER B 587 69.634 14.291 77.712 1.00 34.29 B ATOM 3543 CA SER B 587 69.428 12.870 78.031 1.00 34.28 B ATOM 3544 CB SER B 587 70.548 12.320 78.933 1.00 33.74 B ATOM 3545 OG SER B 587 70.727 13.066 80.122 1.00 34.80 B ATOM 3546 C SER B 587 68.060 12.648 78.685 1.00 33.99 B ATOM 3547 O SER B 587 67.639 13.419 79.546 1.00 32.52 B ATOM 3548 N ALA B 588 67.355 11.615 78.233 1.00 34.19 B ATOM 3549 CA ALA B 588 66.054 11.286 78.793 1.00 35.71 B ATOM 3550 CB ALA B 588 65.006 11.155 77.699 1.00 35.73 B ATOM 3551 C ALA B 588 66.259 9.960 79.495 1.00 36.25 B ATOM 3552 O ALA B 588 66.752 9.016 78.884 1.00 37.28 B ATOM 3553 N SER B 589 65.929 9.906 80.786 1.00 36.81 B ATOM 3554 CA SER B 589 66.084 8.684 81.582 1.00 35.90 B ATOM 3555 CB SER B 589 66.888 8.950 82.851 1.00 34.91 B ATOM 3556 OG SER B 589 66.512 8.030 83.870 1.00 32.54 B ATOM 3557 C SER B 589 64.761 8.093 82.005 1.00 35.49 B ATOM 3558 O SER B 589 63.714 8.712 81.844 1.00 34.24 B ATOM 3559 N MSE B 590 64.826 6.883 82.550 1.00 36.42 B ATOM 3560 CA MSE B 590 63.648 6.188 83.040 1.00 36.64 B ATOM 3561 CB MSE B 590 63.949 4.702 83.249 1.00 39.18 B ATOM 3562 CG MSE B 590 62.896 3.948 84.060 1.00 41.10 B ATOM 3563 SE MSE B 590 63.091 2.012 83.900 1.00 46.30 B ATOM 3564 CE MSE B 590 61.725 1.645 82.565 1.00 45.20 B ATOM 3565 C MSE B 590 63.241 6.819 84.361 1.00 35.83 B ATOM 3566 O MSE B 590 62.152 6.554 84.860 1.00 35.48 B ATOM 3567 N ASP B 591 64.116 7.650 84.932 1.00 35.51 B ATOM 3568 CA ASP B 591 63.791 8.301 86.198 1.00 34.59 B ATOM 3569 CB ASP B 591 65.051 8.767 86.951 1.00 34.80 B ATOM 3570 CG ASP B 591 65.874 9.763 86.177 1.00 34.10 B ATOM 3571 OD1 ASP B 591 65.329 10.459 85.300 1.00 35.66 B ATOM 3572 OD2 ASP B 591 67.081 9.869 86.466 1.00 33.64 B ATOM 3573 C ASP B 591 62.838 9.463 85.986 1.00 33.76 B ATOM 3574 O ASP B 591 62.767 10.373 86.801 1.00 31.76 B ATOM 3575 N THR B 592 62.120 9.418 84.866 1.00 35.29 B ATOM 3576 CA THR B 592 61.120 10.419 84.536 1.00 34.85 B ATOM 3577 CB THR B 592 59.984 10.372 85.631 1.00 34.66 B ATOM 3578 OG1 THR B 592 58.742 10.820 85.079 1.00 38.41 B ATOM 3579 CG2 THR B 592 60.338 11.235 86.830 1.00 34.65 B ATOM 3580 C THR B 592 61.745 11.811 84.403 1.00 33.52 B ATOM 3581 O THR B 592 61.049 12.815 84.455 1.00 33.23 B ATOM 3582 N THR B 593 63.053 11.858 84.169 1.00 32.55 B ATOM 3583 CA THR B 593 63.764 13.130 84.070 1.00 32.86 B ATOM 3584 CB THR B 593 64.786 13.239 85.217 1.00 34.19 B ATOM 3585 OG1 THR B 593 64.082 13.389 86.454 1.00 36.50 B ATOM 3586 CG2 THR B 593 65.730 14.430 85.018 1.00 38.69 B ATOM 3587 C THR B 593 64.500 13.423 82.765 1.00 33.21 B ATOM 3588 O THR B 593 64.856 12.519 82.015 1.00 32.79 B ATOM 3589 N ILE B 594 64.714 14.705 82.488 1.00 33.30 B ATOM 3590 CA ILE B 594 65.471 15.103 81.309 1.00 33.34 B ATOM 3591 CB ILE B 594 64.612 15.829 80.249 1.00 31.46 B ATOM 3592 CG2 ILE B 594 65.496 16.322 79.132 1.00 29.37 B ATOM 3593 CO1 ILE B 594 63.534 14.902 79.690 1.00 32.39 B ATOM 3594 CD1 ILE B 594 62.436 15.642 78.920 1.00 27.89 B ATOM 3595 C ILE B 594 66.497 16.104 81.824 1.00 35.21 B ATOM 3596 O ILE B 594 66.161 16.973 82.628 1.00 37.01 B ATOM 3597 N ARG B 595 67.749 15.977 81.402 1.00 35.67 B ATOM 3598 CA ARG B 595 68.735 16.947 81.834 1.00 36.60 B ATOM 3599 CB ARG B 595 69.447 16.482 83.104 1.00 39.57 B ATOM 3600 CO ARG B 595 70.237 15.219 83.020 1.00 41.84 B ATOM 3601 CD ARG B 595 70.672 14.865 84.428 1.00 43.91 B ATOM 3602 NE ARG B 595 69.554 14.397 85.240 1.00 44.22 B ATOM 3603 CZ ARG B 595 69.658 14.054 86.518 1.00 45.26 B ATOM 3604 NH1 ARG B 595 70.848 14.147 87.121 1.00 44.50 B ATOM 3605 NH2 ARG B 595 68.586 13.589 87.170 1.00 41.38 B ATOM 3606 C ARG B 595 69.731 17.324 80.751 1.00 36.11 B ATOM 3607 O ARG B 595 70.067 16.512 79.880 1.00 36.08 B ATOM 3608 N ILE B 596 70.173 18.579 80.791 1.00 34.47 B ATOM 3609 CA ILE B 596 71.116 19.084 79.807 1.00 34.38 B ATOM 3610 CB ILE B 596 70.662 20.479 79.263 1.00 35.15 B ATOM 3611 CG2 ILE B 596 71.746 21.058 78.357 1.00 35.63 B ATOM 3612 CG1 ILE B 596 69.390 20.334 78.401 1.00 36.12 B ATOM 3613 CD1 ILE B 596 68.175 19.723 79.073 1.00 29.57 B ATOM 3614 C ILE B 596 72.515 19.174 80.415 1.00 32.98 B ATOM 3615 O ILE B 596 72.679 19.563 81.570 1.00 30.78 B ATOM 3616 N TRP B 597 73.520 18.795 79.638 1.00 33.10 B ATOM 3617 CA TRP B 597 74.892 18.821 80.124 1.00 34.71 B ATOM 3618 CB TRP B 597 75.493 17.404 80.117 1.00 34.39 B ATOM 3619 CG TRP B 597 74.577 16.341 80.645 1.00 33.10 B ATOM 3620 CD2 TRP B 597 74.691 15.653 81.893 1.00 33.20 B ATOM 3621 CE2 TRP B 597 73.607 14.752 81.974 1.00 33.38 B ATOM 3622 CE3 TRP B 597 75.599 15.713 82.956 1.00 33.08 B ATOM 3623 CD1 TRP B 597 73.463 15.842 80.035 1.00 33.47 B ATOM 3624 NE1 TRP B 597 72.874 14.884 80.826 1.00 32.94 B ATOM 3625 CZ2 TRP B 597 73.411 13.912 83.072 1.00 33.63 B ATOM 3626 CZ3 TRP B 597 75.406 14.878 84.051 1.00 32.87 B ATOM 3627 CH2 TRP B 597 74.314 13.989 84.101 1.00 33.13 B ATOM 3628 C TRP B 597 75.725 19.726 79.229 1.00 35.90 B ATOM 3629 O TRP B 597 75.455 19.837 78.028 1.00 36.19 B ATOM 3630 N ASP B 598 76.731 20.372 79.817 1.00 36.61 B ATOM 3631 CA ASP B 598 77.631 21.265 79.082 1.00 38.19 B ATOM 3632 CB ASP B 598 78.156 22.369 80.018 1.00 36.98 B ATOM 3633 CG ASP B 598 78.999 23.410 79.291 1.00 37.20 B ATOM 3634 OD1 ASP B 598 79.604 23.089 78.240 1.00 36.53 B ATOM 3635 OD2 ASP B 598 79.059 24.553 79.786 1.00 37.52 B ATOM 3636 C ASP B 598 78.806 20.426 78.574 1.00 39.00 B ATOM 3637 O ASP B 598 79.670 20.050 79.349 1.00 39.73 B ATOM 3638 N LEU B 599 78.847 20.126 77.282 1.00 40.71 B ATOM 3639 CA LEU B 599 79.942 19.320 76.747 1.00 42.08 B ATOM 3640 CB LEU B 599 79.593 18.805 75.344 1.00 40.52 B ATOM 3641 CG LEU B 599 78.606 17.628 75.251 1.00 40.62 B ATOM 3642 CO1 LEU B 599 79.264 16.437 74.600 1.00 38.01 B ATOM 3643 CO2 LEU B 599 78.096 17.258 76.638 1.00 38.10 B ATOM 3644 C LEU B 599 81.295 20.025 76.721 1.00 43.84 B ATOM 3645 O LEU B 599 82.256 19.494 76.165 1.00 44.70 B ATOM 3646 N GLU B 600 81.373 21.216 77.315 1.00 44.72 B ATOM 3647 CA GLU B 600 82.637 21.941 77.358 1.00 45.68 B ATOM 3648 CB GLU B 600 82.412 23.413 77.697 1.00 48.89 B ATOM 3649 CG GLU B 600 83.460 24.367 77.128 1.00 52.63 B ATOM 3650 CD GLU B 600 84.762 24.375 77.924 1.00 56.18 B ATOM 3651 OE1 GLU B 600 84.739 24.763 79.120 1.00 58.19 B ATOM 3652 OE2 GLU B 600 85.811 23.997 77.353 1.00 57.88 B ATOM 3653 C GLU B 600 83.480 21.254 78.419 1.00 45.43 B ATOM 3654 O GLU B 600 84.683 21.083 78.242 1.00 46.22 B ATOM 3655 N ASN B 605 82.844 20.855 79.518 1.00 44.31 B ATOM 3656 CA ASN B 605 83.543 20.124 80.568 1.00 43.89 B ATOM 3657 CB ASN B 605 84.285 21.077 81.520 1.00 46.09 B ATOM 3658 CG ASN B 605 85.808 21.121 81.248 1.00 50.14 B ATOM 3659 OD1 ASN B 605 86.508 20.093 81.348 1.00 50.14 B ATOM 3660 ND2 ASN B 605 86.320 22.314 80.900 1.00 49.96 B ATOM 3661 C ASN B 605 82.630 19.186 81.346 1.00 41.67 B ATOM 3662 O ASN B 605 82.756 19.054 82.554 1.00 43.82 B ATOM 3663 N GLY B 606 81.718 18.525 80.638 1.00 38.96 B ATOM 3664 CA GLY B 606 80.804 17.584 81.268 1.00 35.37 B ATOM 3665 C GLY B 606 80.059 18.044 82.512 1.00 34.56 B ATOM 3666 O GLY B 606 79.668 17.231 83.350 1.00 32.65 B ATOM 3667 N GLU B 607 79.846 19.348 82.622 1.00 34.50 B ATOM 3668 CA GLU B 607 79.147 19.921 83.757 1.00 35.96 B ATOM 3669 CB GLU B 607 79.616 21.367 83.976 1.00 36.06 B ATOM 3670 CG GLU B 607 81.114 21.618 83.763 1.00 39.20 B ATOM 3671 CD GLU B 607 81.468 21.981 82.321 1.00 39.57 B ATOM 3672 OE1 GLU B 607 80.924 21.353 81.405 1.00 41.63 B ATOM 3673 OE2 GLU B 607 82.301 22.877 82.097 1.00 38.72 B ATOM 3674 C GLU B 607 77.622 19.892 83.504 1.00 37.13 B ATOM 3675 O GLU B 607 77.157 20.165 82.391 1.00 36.86 B ATOM 3676 N LEU B 608 76.850 19.539 84.530 1.00 37.44 B ATOM 3677 CA LEU B 608 75.395 19.513 84.412 1.00 37.50 B ATOM 3678 CB LEU B 608 74.753 18.822 85.622 1.00 37.08 B ATOM 3679 CG LEU B 608 73.218 18.925 85.723 1.00 37.03 B ATOM 3680 CD1 LEU B 608 72.593 18.036 84.658 1.00 36.12 B ATOM 3681 CD2 LEU B 608 72.724 18.533 87.127 1.00 34.40 B ATOM 3682 C LEU B 608 74.912 20.962 84.339 1.00 38.65 B ATOM 3683 O LEU B 608 75.442 21.833 85.030 1.00 38.26 B ATOM 3684 N MSE B 625 73.902 21.210 83.510 1.00 39.30 B ATOM 3685 CA MSE B 625 73.368 22.553 83.329 1.00 39.07 B ATOM 3686 CB MSE B 625 73.266 22.890 81.842 1.00 41.00 B ATOM 3687 CG MSE B 625 74.571 23.323 81.217 1.00 43.67 B ATOM 3688 SE MSE B 625 74.423 23.805 79.359 1.00 50.89 B ATOM 3689 CE MSE B 625 73.882 25.650 79.578 1.00 45.39 B ATOM 3690 C MSE B 625 72.008 22.737 83.946 1.00 38.75 B ATOM 3691 O MSE B 625 71.803 23.605 84.795 1.00 39.63 B ATOM 3692 N TYR B 626 71.068 21.919 83.495 1.00 38.88 B ATOM 3693 CA TYR B 626 69.700 22.003 83.975 1.00 37.07 B ATOM 3694 CB TYR B 626 68.861 22.841 83.016 1.00 35.69 B ATOM 3695 CG TYR B 626 69.457 24.160 82.618 1.00 34.35 B ATOM 3696 CD1 TYR B 626 69.560 25.199 83.535 1.00 33.06 B ATOM 3697 CE1 TYR B 626 70.013 26.447 83.150 1.00 32.14 B ATOM 3698 CD2 TYR B 626 69.840 24.397 81.295 1.00 34.51 B ATOM 3699 CE2 TYR B 626 70.296 25.646 80.896 1.00 33.07 B ATOM 3700 CZ TYR B 626 70.373 26.671 81.833 1.00 31.79 B ATOM 3701 OH TYR B 626 70.753 27.933 81.446 1.00 28.57 B ATOM 3702 C TYR B 626 69.067 20.635 84.040 1.00 36.34 B ATOM 3703 O TYR B 626 69.528 19.690 83.410 1.00 37.33 B ATOM 3704 N THR B 627 67.992 20.560 84.809 1.00 36.28 B ATOM 3705 CA THR B 627 67.203 19.357 84.958 1.00 34.33 B ATOM 3706 CB THR B 627 67.340 18.744 86.373 1.00 32.94 B ATOM 3707 OG1 THR B 627 68.684 18.292 86.562 1.00 30.38 B ATOM 3708 CG2 THR B 627 66.391 17.544 86.535 1.00 32.04 B ATOM 3709 C THR B 627 65.764 19.808 84.719 1.00 34.24 B ATOM 3710 O THR B 627 65.248 20.700 85.400 1.00 33.46 B ATOM 3711 N LEU B 628 65.137 19.204 83.722 1.00 34.53 B ATOM 3712 CA LEU B 628 63.772 19.525 83.355 1.00 34.30 B ATOM 3713 CB LEU B 628 63.636 19.558 81.835 1.00 35.54 B ATOM 3714 CG LEU B 628 64.814 20.120 81.056 1.00 36.04 B ATOM 3715 CO1 LEU B 628 64.459 20.071 79.591 1.00 37.79 B ATOM 3716 CD2 LEU B 628 65.137 21.538 81.500 1.00 35.35 B ATOM 3717 C LEU B 628 62.844 18.454 83.886 1.00 32.68 B ATOM 3718 O LEU B 628 63.055 17.261 83.647 1.00 33.72 B ATOM 3719 N GLN B 629 61.805 18.882 84.582 1.00 30.62 B ATOM 3720 CA GLN B 629 60.849 17.949 85.127 1.00 30.70 B ATOM 3721 CB GLN B 629 60.774 18.082 86.647 1.00 28.58 B ATOM 3722 CG GLN B 629 59.867 17.050 87.257 1.00 27.57 B ATOM 3723 CD GLN B 629 60.402 15.655 87.063 1.00 28.68 B ATOM 3724 OE1 GLN B 629 59.733 14.775 86.486 1.00 28.51 B ATOM 3725 NE2 GLN B 629 61.620 15.434 87.545 1.00 27.17 B ATOM 3726 C GLN B 629 59.473 18.204 84.544 1.00 31.36 B ATOM 3727 O GLN B 629 58.677 18.958 85.104 1.00 31.90 B ATOM 3728 N GLY B 630 59.183 17.567 83.424 1.00 31.87 B ATOM 3729 CA GLY B 630 57.889 17.767 82.804 1.00 33.15 B ATOM 3730 C GLY B 630 57.254 16.467 82.364 1.00 33.55 B ATOM 3731 O GLY B 630 56.511 16.425 81.385 1.00 35.60 B ATOM 3732 N HIS B 631 57.553 15.400 83.092 1.00 32.53 B ATOM 3733 CA HIS B 631 57.023 14.083 82.784 1.00 30.78 B ATOM 3734 CB HIS B 631 57.943 13.368 81.792 1.00 28.27 B ATOM 3735 CG HIS B 631 58.054 14.052 80.466 1.00 24.31 B ATOM 3736 CD2 HIS B 631 59.003 14.874 79.965 1.00 21.91 B ATOM 3737 ND1 HIS B 631 57.118 13.895 79.467 1.00 26.41 B ATOM 3738 CE1 HIS B 631 57.487 14.587 78.405 1.00 22.90 B ATOM 3739 NE2 HIS B 631 58.629 15.190 78.681 1.00 22.42 B ATOM 3740 C HIS B 631 56.957 13.302 84.091 1.00 30.77 B ATOM 3741 O HIS B 631 57.834 13.437 84.948 1.00 30.31 B ATOM 3742 N THR B 632 55.916 12.489 84.239 1.00 31.40 B ATOM 3743 CA THR B 632 55.716 11.690 85.447 1.00 32.08 B ATOM 3744 CB THR B 632 54.281 11.742 85.914 1.00 32.58 B ATOM 3745 OG1 THR B 632 53.446 11.255 84.860 1.00 33.44 B ATOM 3746 CG2 THR B 632 53.877 13.151 86.274 1.00 31.80 B ATOM 3747 C THR B 632 55.990 10.233 85.152 1.00 32.55 B ATOM 3748 O THR B 632 55.790 9.367 86.000 1.00 33.19 B ATOM 3749 N ALA B 633 56.442 9.963 83.941 1.00 32.22 B ATOM 3750 CA ALA B 633 56.721 8.604 83.537 1.00 32.78 B ATOM 3751 CB ALA B 633 55.596 8.106 82.627 1.00 33.46 B ATOM 3752 C ALA B 633 58.048 8.649 82.786 1.00 33.18 B ATOM 3753 O ALA B 633 58.570 9.730 82.526 1.00 34.34 B ATOM 3754 N LEU B 634 58.606 7.502 82.419 1.00 32.23 B ATOM 3755 CA LEU B 634 59.881 7.559 81.718 1.00 31.56 B ATOM 3756 CE LEU B 634 60.531 6.176 81.610 1.00 32.84 B ATOM 3757 CG LEU B 634 59.855 5.099 80.783 1.00 33.81 B ATOM 3758 CD1 LEU B 634 58.372 5.151 81.095 1.00 37.82 B ATOM 3759 CD2 LEU B 634 60.122 5.300 79.304 1.00 32.77 B ATOM 3760 C LEU B 634 59.787 8.214 80.353 1.00 29.60 B ATOM 3761 O LEU B 634 58.807 8.072 79.620 1.00 27.99 B ATOM 3762 N VAL B 635 60.835 8.961 80.045 1.00 27.96 B ATOM 3763 CA VAL B 635 60.945 9.688 78.803 1.00 25.69 B ATOM 3764 CB VAL B 635 61.584 11.046 79.038 1.00 27.20 B ATOM 3765 CG1 VAL B 635 61.377 11.926 77.810 1.00 28.07 B ATOM 3766 CG2 VAL B 635 61.000 11.679 80.302 1.00 25.75 B ATOM 3767 C VAL B 635 61.827 8.948 77.840 1.00 23.61 B ATOM 3768 O VAL B 635 63.046 9.033 77.942 1.00 23.52 B ATOM 3769 N GLY B 636 61.219 8.248 76.891 1.00 22.88 B ATOM 3770 CA GLY B 636 61.998 7.488 75.928 1.00 22.35 B ATOM 3771 C GLY B 636 62.224 8.089 74.550 1.00 23.37 B ATOM 3772 O GLY B 636 62.907 7.480 73.736 1.00 24.09 B ATOM 3773 N LEU B 637 61.656 9.262 74.277 1.00 23.96 B ATOM 3774 CA LEU B 637 61.827 9.904 72.981 1.00 23.22 B ATOM 3775 CB LEU B 637 60.503 9.934 72.228 1.00 22.08 B ATOM 3776 CG LEU B 637 59.913 8.534 72.102 1.00 21.07 B ATOM 3777 CD1 LEU B 637 58.494 8.554 71.516 1.00 18.52 B ATOM 3778 CD2 LEU B 637 60.863 7.724 71.261 1.00 18.91 B ATOM 3779 C LEU B 637 62.328 11.317 73.164 1.00 25.24 B ATOM 3780 O LEU B 637 62.058 11.945 74.197 1.00 25.36 B ATOM 3781 N LEU B 638 63.048 11.797 72.142 1.00 26.06 B ATOM 3782 CA LEU B 638 63.635 13.147 72.077 1.00 25.52 B ATOM 3783 CB LEU B 638 64.907 13.258 72.926 1.00 25.76 B ATOM 3784 CG LEU B 638 64.857 13.321 74.453 1.00 26.07 B ATOM 3785 CD1 LEU B 638 66.285 13.384 74.983 1.00 27.82 B ATOM 3786 CD2 LEU B 638 64.073 14.535 74.897 1.00 25.88 B ATOM 3787 C LEU B 638 64.022 13.494 70.653 1.00 25.17 B ATOM 3788 O LEU B 638 64.529 12.644 69.919 1.00 25.44 B ATOM 3789 N ARG B 639 63.771 14.744 70.268 1.00 25.50 B ATOM 3790 CA ARG B 639 64.126 15.260 68.942 1.00 25.66 B ATOM 3791 CB ARG B 639 63.033 14.936 67.901 1.00 25.21 B ATOM 3792 CG ARG B 639 62.720 13.427 67.878 1.00 28.60 B ATOM 3793 CD ARG B 639 62.173 12.811 66.583 1.00 28.49 B ATOM 3794 NE ARG B 639 63.252 12.293 65.730 1.00 30.47 B ATOM 3795 CZ ARG B 639 63.131 11.295 64.851 1.00 30.02 B ATOM 3796 NH1 ARG B 639 61.970 10.668 64.684 1.00 27.71 B ATOM 3797 NH2 ARG B 639 64.183 10.926 64.123 1.00 32.50 B ATOM 3798 C ARG B 639 64.379 16.760 69.078 1.00 25.33 B ATOM 3799 O ARG B 639 63.738 17.442 69.877 1.00 24.41 B ATOM 3800 N LEU B 640 65.355 17.258 68.332 1.00 26.36 B ATOM 3801 CA LEU B 640 65.707 18.661 68.408 1.00 27.00 B ATOM 3802 CB LEU B 640 67.214 18.808 68.563 1.00 28.00 B ATOM 3803 CG LEU B 640 67.688 19.504 69.834 1.00 27.72 B ATOM 3804 CD1 LEU B 640 69.188 19.757 69.737 1.00 25.31 B ATOM 3805 CD2 LEU B 640 66.914 20.802 70.019 1.00 25.63 B ATOM 3806 C LEU B 640 65.263 19.432 67.189 1.00 27.04 B ATOM 3807 O LEU B 640 65.759 19.210 66.097 1.00 27.98 B ATOM 3808 N SER B 641 64.310 20.329 67.373 1.00 29.24 B ATOM 3809 CA SER B 641 63.828 21.138 66.271 1.00 30.57 B ATOM 3810 CB SER B 641 62.359 21.509 66.504 1.00 31.54 B ATOM 3811 OG SER B 641 62.025 22.763 65.944 1.00 30.17 B ATOM 3812 C SER B 641 64.718 22.366 66.277 1.00 31.05 B ATOM 3813 O SER B 641 65.499 22.560 67.198 1.00 32.13 B ATOM 3814 N ASP B 642 64.628 23.194 65.254 1.00 32.29 B ATOM 3815 CA ASP B 642 65.472 24.373 65.210 1.00 32.45 B ATOM 3816 CB ASP B 642 65.293 25.059 63.870 1.00 36.58 B ATOM 3817 CG ASP B 642 66.575 25.652 63.360 1.00 40.19 B ATOM 3818 OD1 ASP B 642 67.336 24.914 62.681 1.00 41.18 B ATOM 3819 OD2 ASP B 642 66.816 26.848 63.661 1.00 42.03 B ATOM 3820 C ASP B 642 65.140 25.348 66.344 1.00 31.30 B ATOM 3821 O ASP B 642 65.996 26.095 66.809 1.00 28.33 B ATOM 3822 N LYS B 643 63.876 25.332 66.759 1.00 30.65 B ATOM 3823 CA LYS B 643 63.373 26.190 67.818 1.00 28.54 B ATOM 3824 CB LYS B 643 62.069 26.888 67.407 1.00 28.11 B ATOM 3825 CG LYS B 643 62.141 27.807 66.210 1.00 30.60 B ATOM 3826 CD LYS B 643 63.196 28.902 66.364 1.00 32.54 B ATOM 3827 CE LYS B 643 63.332 29.736 65.070 1.00 33.58 B ATOM 3828 NZ LYS B 643 63.760 28.917 63.873 1.00 33.86 B ATOM 3829 C LYS B 643 63.047 25.391 69.077 1.00 28.15 B ATOM 3830 O LYS B 643 63.019 25.951 70.163 1.00 28.92 B ATOM 3831 N PHE B 644 62.787 24.094 68.957 1.00 26.09 B ATOM 3832 CA PHE B 644 62.413 23.353 70.152 1.00 24.49 B ATOM 3833 CB PHE B 644 60.931 22.958 70.115 1.00 21.46 B ATOM 3834 CG PHE B 644 60.015 24.023 69.613 1.00 20.17 B ATOM 3835 CD1 PHE B 644 59.720 24.125 68.258 1.00 22.46 B ATOM 3836 CD2 PHE B 644 59.404 24.896 70.493 1.00 20.58 B ATOM 3837 CE1 PHE B 644 58.816 25.079 67.783 1.00 20.21 B ATOM 3838 CE2 PHE B 644 58.501 25.855 70.035 1.00 20.45 B ATOM 3839 CZ PHE B 644 58.207 25.942 68.674 1.00 20.84 B ATOM 3840 C PHE B 644 63.186 22.087 70.457 1.00 25.20 B ATOM 3841 O PHE B 644 63.886 21.534 69.613 1.00 24.80 B ATOM 3842 N LEU B 645 63.054 21.649 71.701 1.00 25.69 B ATOM 3843 CA LEU B 645 63.630 20.396 72.151 1.00 25.88 B ATOM 3844 CB LEU B 645 64.547 20.586 73.359 1.00 26.05 B ATOM 3845 CG LEU B 645 64.777 19.327 74.233 1.00 27.77 B ATOM 3846 CD1 LEU B 645 66.044 18.602 73.852 1.00 28.34 B ATOM 3847 CD2 LEU B 645 64.864 19.739 75.692 1.00 29.93 B ATOM 3848 C LEU B 645 62.349 19.704 72.590 1.00 26.32 B ATOM 3849 O LEU B 645 61.743 20.096 73.591 1.00 27.97 B ATOM 3850 N VAL B 646 61.910 18.706 71.834 1.00 25.54 B ATOM 3851 CA VAL B 646 60.688 18.005 72.191 1.00 25.91 B ATOM 3852 CB VAL B 646 59.892 17.651 70.918 1.00 25.69 B ATOM 3853 CG1 VAL B 646 58.554 17.036 71.293 1.00 26.37 B ATOM 3854 CG2 VAL B 646 59.681 18.909 70.069 1.00 23.92 B ATOM 3855 C VAL B 646 61.003 16.734 72.986 1.00 26.60 B ATOM 3856 O VAL B 646 62.051 16.130 72.780 1.00 27.76 B ATOM 3857 N SER B 647 60.121 16.358 73.916 1.00 27.17 B ATOM 3858 CA SER B 647 60.281 15.130 74.711 1.00 27.29 B ATOM 3859 CB SER B 647 60.956 15.417 76.054 1.00 27.08 B ATOM 3860 OG SER B 647 60.210 16.325 76.850 1.00 27.93 B ATOM 3861 C SER B 647 58.905 14.512 74.942 1.00 28.49 B ATOM 3862 O SER B 647 57.943 15.227 75.219 1.00 29.23 B ATOM 3863 N ALA B 648 58.819 13.189 74.800 1.00 28.67 B ATOM 3864 CA ALA B 648 57.568 12.454 74.976 1.00 28.62 B ATOM 3865 CB ALA B 648 57.093 11.906 73.630 1.00 28.17 B ATOM 3866 C ALA B 648 57.760 11.306 75.972 1.00 30.51 B ATOM 3867 O ALA B 648 58.756 10.577 75.898 1.00 31.42 B ATOM 3868 N ALA B 649 56.807 11.146 76.894 1.00 30.32 B ATOM 3869 CA ALA B 649 56.883 10.098 77.911 1.00 30.33 B ATOM 3870 CB ALA B 649 56.720 10.700 79.305 1.00 29.35 B ATOM 3871 C ALA B 649 55.863 8.988 77.711 1.00 31.09 B ATOM 3872 O ALA B 649 54.995 9.080 76.850 1.00 30.54 B ATOM 3873 N ALA B 650 55.981 7.941 78.530 1.00 32.95 B ATOM 3874 CA ALA B 650 55.103 6.768 78.483 1.00 32.69 B ATOM 3875 CB ALA B 650 55.783 5.597 79.194 1.00 30.66 B ATOM 3876 C ALA B 650 53.733 7.019 79.098 1.00 33.02 B ATOM 3877 O ALA B 650 52.941 6.091 79.251 1.00 32.69 B ATOM 3878 N ASP B 651 53.471 8.270 79.463 1.00 34.34 B ATOM 3879 CA ASP B 651 52.200 8.661 80.063 1.00 35.15 B ATOM 3880 CB ASP B 651 52.456 9.528 81.287 1.00 36.84 B ATOM 3881 CG ASP B 651 53.402 10.663 80.993 1.00 40.07 B ATOM 3882 OD1 ASP B 651 53.652 10.935 79.800 1.00 40.99 B ATOM 3883 OD2 ASP B 651 53.895 11.299 81.950 1.00 43.26 B ATOM 3884 C ASP B 651 51.347 9.441 79.068 1.00 35.49 B ATOM 3885 O ASP B 651 50.282 9.948 79.418 1.00 35.89 B ATOM 3886 N GLY B 652 51.833 9.542 77.834 1.00 34.99 B ATOM 3887 CA GLY B 652 51.110 10.260 76.802 1.00 34.08 B ATOM 3888 C GLY B 652 51.434 11.738 76.730 1.00 34.36 B ATOM 3889 O GLY B 652 50.877 12.449 75.891 1.00 36.08 B ATOM 3890 N SER B 653 52.336 12.198 77.595 1.00 32.03 B ATOM 3891 CA SER B 653 52.720 13.605 77.635 1.00 30.49 B ATOM 3892 CB SER B 653 53.176 13.995 79.050 1.00 31.53 B ATOM 3893 OG SER B 653 54.387 13.358 79.428 1.00 31.63 B ATOM 3894 C SER B 653 53.810 13.962 76.633 1.00 29.75 B ATOM 3895 O SER B 653 54.702 13.165 76.361 1.00 28.99 B ATOM 3896 N ILE B 654 53.733 15.175 76.097 1.00 30.15 B ATOM 3897 CA ILE B 654 54.703 15.655 75.115 1.00 30.00 B ATOM 3898 CB ILE B 654 54.083 15.708 73.706 1.00 29.09 B ATOM 3899 CG2 ILE B 654 55.115 16.144 72.686 1.00 28.47 B ATOM 3900 CG1 ILE B 654 53.548 14.336 73.318 1.00 28.15 B ATOM 3901 CD1 ILE B 654 52.204 14.400 72.675 1.00 30.38 B ATOM 3902 C ILE B 654 55.109 17.061 75.508 1.00 30.87 B ATOM 3903 O ILE B 654 54.285 17.974 75.484 1.00 32.52 B ATOM 3904 N ARG B 655 56.371 17.241 75.878 1.00 30.22 B ATOM 3905 CA ARG B 655 56.835 18.570 76.271 1.00 29.48 B ATOM 3906 CB ARG B 655 57.614 18.492 77.589 1.00 31.26 B ATOM 3907 CG ARG B 655 56.773 18.219 78.827 1.00 34.00 B ATOM 3908 CD ARG B 655 56.140 19.500 79.287 1.00 40.70 B ATOM 3909 NE ARG B 655 55.601 19.484 80.657 1.00 45.23 B ATOM 3910 CZ ARG B 655 54.582 18.735 81.075 1.00 48.41 B ATOM 3911 NH1 ARG B 655 53.979 17.909 80.234 1.00 49.81 B ATOM 3912 NH2 ARG B 655 54.137 18.847 82.324 1.00 50.20 B ATOM 3913 C ARG B 655 57.712 19.195 75.187 1.00 28.14 B ATOM 3914 O ARG B 655 58.462 18.501 74.500 1.00 27.90 B ATOM 3915 N GLY B 656 57.582 20.507 75.033 1.00 26.00 B ATOM 3916 CA GLY B 656 58.365 21.237 74.065 1.00 24.28 B ATOM 3917 C GLY B 656 59.047 22.348 74.830 1.00 24.73 B ATOM 3918 O GLY B 656 58.384 23.228 75.386 1.00 26.11 B ATOM 3919 N TRP B 657 60.373 22.296 74.883 1.00 24.11 B ATOM 3920 CA TRP B 657 61.163 23.294 75.601 1.00 23.50 B ATOM 3921 CB TRP B 657 62.139 22.602 76.550 1.00 22.75 B ATOM 3922 CG TRP B 657 61.579 21.381 77.189 1.00 21.95 B ATOM 3923 CD2 TRP B 657 61.213 21.230 78.562 1.00 19.79 B ATOM 3924 CE2 TRP B 657 60.639 19.948 78.698 1.00 20.88 B ATOM 3925 CE3 TRP B 657 61.320 22.048 79.691 1.00 19.86 B ATOM 3926 CD1 TRP B 657 61.231 20.213 76.566 1.00 20.79 B ATOM 3927 NE1 TRP B 657 60.657 19.350 77.469 1.00 20.21 B ATOM 3928 CZ2 TRP B 657 60.160 19.478 79.926 1.00 21.49 B ATOM 3929 CZ3 TRP B 657 60.846 21.570 80.915 1.00 20.44 B ATOM 3930 CR2 TRP B 657 60.278 20.301 81.019 1.00 20.36 B ATOM 3931 C TRP B 657 61.966 24.122 74.610 1.00 24.96 B ATOM 3932 O TRP B 657 62.262 23.673 73.498 1.00 24.34 B ATOM 3933 N ASP B 658 62.331 25.331 75.014 1.00 26.03 B ATOM 3934 CA ASP B 658 63.126 26.181 74.137 1.00 28.03 B ATOM 3935 CB ASP B 658 63.307 27.565 74.741 1.00 28.12 B ATOM 3936 CG ASP B 658 64.031 28.494 73.805 1.00 29.75 B ATOM 3937 OD1 ASP B 658 65.264 28.356 73.641 1.00 28.58 B ATOM 3938 OD2 ASP B 658 63.352 29.351 73.209 1.00 31.24 B ATOM 3939 C ASP B 658 64.498 25.538 73.961 1.00 28.55 B ATOM 3940 O ASP B 658 65.168 25.253 74.948 1.00 31.11 B ATOM 3941 N ALA B 659 64.924 25.334 72.719 1.00 27.30 B ATOM 3942 CA ALA B 659 66.209 24.689 72.443 1.00 28.28 B ATOM 3943 CB ALA B 659 66.413 24.549 70.945 1.00 26.59 B ATOM 3944 C ALA B 659 67.430 25.362 73.047 1.00 29.08 B ATOM 3945 O ALA B 659 68.518 24.784 73.067 1.00 30.37 B ATOM 3946 N ASN B 660 67.272 26.577 73.544 1.00 29.04 B ATOM 3947 CA ASN B 660 68.419 27.256 74.090 1.00 29.15 B ATOM 3948 CB ASN B 660 68.618 28.573 73.361 1.00 32.02 B ATOM 3949 CG ASN B 660 69.953 29.185 73.646 1.00 36.15 B ATOM 3950 OD1 ASN B 660 70.999 28.600 73.342 1.00 39.04 B ATOM 3951 ND2 ASN B 660 69.939 30.371 74.238 1.00 38.31 B ATOM 3952 C ASN B 660 68.334 27.474 75.582 1.00 28.96 B ATOM 3953 O ASN B 660 69.262 27.138 76.301 1.00 30.76 B ATOM 3954 N ASP B 661 67.225 28.024 76.059 1.00 28.20 B ATOM 3955 CA ASP B 661 67.073 28.249 77.485 1.00 26.87 B ATOM 3956 CB ASP B 661 66.553 29.663 77.745 1.00 29.19 B ATOM 3957 CG ASP B 661 65.311 29.984 76.942 1.00 30.92 B ATOM 3958 OD1 ASP B 661 65.314 31.019 76.232 1.00 32.39 B ATOM 3959 OD2 ASP B 661 64.334 29.209 77.023 1.00 30.85 B ATOM 3960 C ASP B 661 66.147 27.217 78.129 1.00 26.15 B ATOM 3961 O ASP B 661 66.041 27.165 79.346 1.00 28.27 B ATOM 3962 N TYR B 662 65.474 26.409 77.317 1.00 22.94 B ATOM 3963 CA TYR B 662 64.590 25.365 77.819 1.00 21.57 B ATOM 3964 CB TYR B 662 65.407 24.340 78.623 1.00 20.55 B ATOM 3965 CG TYR B 662 66.647 23.879 77.871 1.00 21.52 B ATOM 3966 CD1 TYR B 662 67.867 24.533 78.019 1.00 19.76 B ATOM 3967 CE1 TYR B 662 68.960 24.193 77.231 1.00 18.58 B ATOM 3968 CD2 TYR B 662 66.567 22.861 76.919 1.00 20.80 B ATOM 3969 CE2 TYR B 662 67.659 22.519 76.126 1.00 18.36 B ATOM 3970 CZ TYR B 662 68.851 23.192 76.287 1.00 18.65 B ATOM 3971 OH TYR B 662 69.935 22.893 75.493 1.00 18.77 B ATOM 3972 C TYR B 662 63.346 25.808 78.604 1.00 21.16 B ATOM 3973 O TYR B 662 62.835 25.068 79.443 1.00 20.62 B ATOM 3974 N SER B 663 62.864 27.015 78.327 1.00 21.52 B ATOM 3975 CA SER B 663 61.642 27.500 78.954 1.00 21.24 B ATOM 3976 CB SER B 663 61.458 28.993 78.699 1.00 19.14 B ATOM 3977 OG SER B 663 61.441 29.273 77.312 1.00 19.19 B ATOM 3978 C SER B 663 60.496 26.728 78.294 1.00 21.60 B ATOM 3979 O SER B 663 60.585 26.352 77.123 1.00 20.87 B ATOM 3980 N ARG B 664 59.436 26.489 79.057 1.00 22.75 B ATOM 3981 CA ARG B 664 58.267 25.755 78.592 1.00 23.75 B ATOM 3982 CB ARG B 664 57.317 25.544 79.764 1.00 26.18 B ATOM 3983 CG ARG B 664 58.032 24.928 80.948 1.00 33.56 B ATOM 3984 CD ARG B 664 57.130 24.061 81.812 1.00 39.29 B ATOM 3985 NE ARG B 664 57.925 23.331 82.801 1.00 43.83 B ATOM 3986 CZ ARG B 664 57.446 22.404 83.625 1.00 47.40 B ATOM 3987 NH1 ARG B 664 56.158 22.076 83.594 1.00 48.81 B ATOM 3988 NH2 ARG B 664 58.265 21.796 84.474 1.00 48.40 B ATOM 3989 C ARG B 664 57.540 26.436 77.433 1.00 23.79 B ATOM 3990 O ARG B 664 56.829 27.420 77.632 1.00 23.72 B ATOM 3991 N LYS B 665 57.702 25.886 76.228 1.00 23.87 B ATOM 3992 CA LYS B 665 57.091 26.453 75.021 1.00 24.18 B ATOM 3993 CB LYS B 665 58.099 26.400 73.869 1.00 25.26 B ATOM 3994 CG LYS B 665 59.088 27.551 73.869 1.00 26.13 B ATOM 3995 CD LYS B 665 58.423 28.779 73.292 1.00 31.91 B ATOM 3996 CE LYS B 665 59.389 29.964 73.126 1.00 34.51 B ATOM 3997 NZ LYS B 665 59.804 30.608 74.426 1.00 40.98 B ATOM 3998 C LYS B 665 55.760 25.844 74.588 1.00 22.25 B ATOM 3999 O LYS B 665 54.943 26.514 73.956 1.00 21.84 B ATOM 4000 N PHE B 666 55.555 24.574 74.917 1.00 22.07 B ATOM 4001 CA PHE B 666 54.308 23.875 74.604 1.00 22.00 B ATOM 4002 CB PHE B 666 54.109 23.776 73.076 1.00 21.53 B ATOM 4003 CG PHE B 666 55.017 22.786 72.373 1.00 21.45 B ATOM 4004 CD1 PHE B 666 54.744 21.420 72.408 1.00 21.12 B ATOM 4005 CD2 PHE B 666 56.134 23.218 71.664 1.00 20.63 B ATOM 4006 CE1 PHE B 666 55.562 20.506 71.758 1.00 17.08 B ATOM 4007 CE2 PHE B 666 56.951 22.303 71.015 1.00 19.89 B ATOM 4008 CZ PHE B 666 56.659 20.947 71.066 1.00 17.19 B ATOM 4009 C PHE B 666 54.272 22.494 75.288 1.00 22.61 B ATOM 4010 O PHE B 666 55.323 21.938 75.618 1.00 24.01 B ATOM 4011 N SER B 667 53.068 21.973 75.538 1.00 22.74 B ATOM 4012 CA SER B 667 52.891 20.674 76.200 1.00 23.29 B ATOM 4013 CB SER B 667 52.827 20.831 77.717 1.00 22.23 B ATOM 4014 OG SER B 667 51.487 20.937 78.145 1.00 23.02 B ATOM 4015 C SER B 667 51.596 20.014 75.737 1.00 24.06 B ATOM 4016 O SER B 667 50.525 20.635 75.772 1.00 23.18 B ATOM 4017 N TYR B 668 51.703 18.751 75.321 1.00 24.19 B ATOM 4018 CA TYR B 668 50.554 17.999 74.834 1.00 24.45 B ATOM 4019 CB TYR B 668 50.633 17.810 73.324 1.00 24.25 B ATOM 4020 CG TYR B 668 50.638 19.089 72.543 1.00 24.38 B ATOM 4021 CD1 TYR B 668 51.752 19.452 71.785 1.00 23.71 B ATOM 4022 CE1 TYR B 668 51.759 20.610 71.024 1.00 24.24 B ATOM 4023 CD2 TYR B 668 49.519 19.924 72.528 1.00 24.84 B ATOM 4024 CE2 TYR B 668 49.514 21.091 71.770 1.00 25.84 B ATOM 4025 CZ TYR B 668 50.643 21.426 71.017 1.00 26.29 B ATOM 4026 OH TYR B 668 50.656 22.572 70.263 1.00 27.29 B ATOM 4027 C TYR B 668 50.391 16.634 75.462 1.00 23.76 B ATOM 4028 O TYR B 668 51.364 15.944 75.751 1.00 23.84 B ATOM 4029 N HIS B 669 49.144 16.223 75.612 1.00 24.21 B ATOM 4030 CA HIS B 669 48.864 14.948 76.225 1.00 26.26 B ATOM 4031 CB HIS B 669 48.329 15.214 77.623 1.00 27.79 B ATOM 4032 CG HIS B 669 48.682 14.159 78.607 1.00 30.20 B ATOM 4033 CD2 HIS B 669 48.174 12.921 78.797 1.00 32.47 B ATOM 4034 ND1 HIS B 669 49.695 14.309 79.526 1.00 30.16 B ATOM 4035 CE1 HIS B 669 49.796 13.205 80.244 1.00 31.69 B ATOM 4036 NE2 HIS B 669 48.884 12.347 79.822 1.00 32.65 B ATOM 4037 C HIS B 669 47.836 14.157 75.421 1.00 25.01 B ATOM 4038 O HIS B 669 46.743 14.662 75.167 1.00 25.41 B ATOM 4039 N HIS B 670 48.163 12.936 75.003 1.00 24.99 B ATOM 4040 CA HIS B 670 47.173 12.152 74.262 1.00 26.67 B ATOM 4041 CB HIS B 670 47.788 10.894 73.644 1.00 26.67 B ATOM 4042 CG HIS B 670 48.526 11.149 72.367 1.00 28.25 B ATOM 4043 CD2 HIS B 670 49.149 12.266 71.911 1.00 27.02 B ATOM 4044 ND1 HIS B 670 48.704 10.187 71.399 1.00 28.10 B ATOM 4045 CE1 HIS B 670 49.404 10.697 70.398 1.00 27.39 B ATOM 4046 NE2 HIS B 670 49.685 11.955 70.687 1.00 25.82 B ATOM 4047 C HIS B 670 46.033 11.766 75.198 1.00 28.34 B ATOM 4048 O HIS B 670 46.255 11.292 76.320 1.00 28.98 B ATOM 4049 N THR B 671 44.812 11.970 74.717 1.00 29.18 B ATOM 4050 CA THR B 671 43.597 11.706 75.479 1.00 29.09 B ATOM 4051 CB THR B 671 42.363 11.963 74.600 1.00 28.97 B ATOM 4052 OG1 THR B 671 42.582 11.400 73.299 1.00 29.48 B ATOM 4053 CG2 THR B 671 42.108 13.457 74.470 1.00 28.78 B ATOM 4054 C THR B 671 43.434 10.341 76.127 1.00 27.51 B ATOM 4055 O THR B 671 42.911 10.245 77.234 1.00 26.92 B ATOM 4056 N ASN B 672 43.857 9.291 75.436 1.00 28.14 B ATOM 4057 CA ASN B 672 43.715 7.936 75.961 1.00 29.14 B ATOM 4058 CB ASN B 672 43.528 6.943 74.808 1.00 30.07 B ATOM 4059 CG ASN B 672 44.774 6.802 73.954 1.00 31.70 B ATOM 4060 OD1 ASN B 672 45.721 7.592 74.082 1.00 32.55 B ATOM 4061 ND2 ASN B 672 44.779 5.803 73.067 1.00 30.68 B ATOM 4062 C ASN B 672 44.911 7.538 76.819 1.00 27.80 B ATOM 4063 O ASN B 672 45.184 6.354 77.040 1.00 25.74 B ATOM 4064 N LEU B 673 45.624 8.554 77.283 1.00 27.49 B ATOM 4065 CA LEU B 673 46.771 8.370 78.152 1.00 28.57 B ATOM 4066 CB LEU B 673 46.267 8.132 79.581 1.00 26.43 B ATOM 4067 CG LEU B 673 45.295 9.183 80.132 1.00 27.88 B ATOM 4068 CD1 LEU B 673 44.949 8.826 81.572 1.00 28.51 B ATOM 4069 CD2 LEU B 673 45.898 10.581 80.067 1.00 26.47 B ATOM 4070 C LEU B 673 47.711 7.243 77.727 1.00 28.78 B ATOM 4071 O LEU B 673 48.353 6.613 78.560 1.00 28.06 B ATOM 4072 N SER B 674 47.805 6.992 76.431 1.00 29.36 B ATOM 4073 CA SER B 674 48.676 5.926 75.960 1.00 29.70 B ATOM 4074 CB SER B 674 48.207 5.459 74.585 1.00 32.41 B ATOM 4075 OG SER B 674 46.859 5.039 74.652 1.00 35.35 B ATOM 4076 G SER B 674 50.140 6.353 75.892 1.00 27.54 B ATOM 4077 O SER B 674 50.438 7.522 75.678 1.00 27.24 B ATOM 4078 N ALA B 675 51.053 5.407 76.074 1.00 25.24 B ATOM 4079 CA ALA B 675 52.455 5.748 76.006 1.00 24.53 B ATOM 4080 CB ALA B 675 53.304 4.573 76.393 1.00 25.14 B ATOM 4081 C ALA B 675 52.793 6.179 74.589 1.00 25.51 B ATOM 4082 O ALA B 675 52.484 5.472 73.610 1.00 26.90 B ATOM 4083 N ILE B 676 53.429 7.340 74.485 1.00 23.80 B ATOM 4084 CA ILE B 676 53.824 7.880 73.200 1.00 23.18 B ATOM 4085 CB ILE B 676 54.457 9.276 73.354 1.00 22.28 B ATOM 4086 CG2 ILE B 676 54.960 9.749 71.999 1.00 26.37 B ATOM 4087 CG1 ILE B 676 53.437 10.265 73.913 1.00 20.36 B ATOM 4088 CD1 ILE B 676 52.158 10.388 73.112 1.00 19.30 B ATOM 4089 C ILE B 676 54.835 6.966 72.505 1.00 23.03 B ATOM 4090 O ILE B 676 55.939 6.770 73.005 1.00 22.66 B ATOM 4091 N THR B 677 54.454 6.432 71.344 1.00 23.91 B ATOM 4092 CA THR B 677 55.310 5.536 70.554 1.00 24.45 B ATOM 4093 CB THR B 677 54.495 4.625 69.663 1.00 21.85 B ATOM 4094 OG1 THR B 677 53.512 3.966 70.447 1.00 21.96 B ATOM 4095 CG2 THR B 677 55.406 3.590 69.020 1.00 27.86 B ATOM 4096 C THR B 677 56.291 6.286 69.642 1.00 26.36 B ATOM 4097 O THR B 677 57.469 5.953 69.580 1.00 26.98 B ATOM 4098 N THR B 678 55.787 7.252 68.884 1.00 27.47 B ATOM 4099 CA THR B 678 56.647 8.070 68.046 1.00 28.85 B ATOM 4100 CB THR B 678 56.939 7.483 66.615 1.00 31.08 B ATOM 4101 OG1 THR B 678 55.731 7.007 66.003 1.00 33.29 B ATOM 4102 CG2 THR B 678 57.971 6.378 66.698 1.00 35.12 B ATOM 4103 C THR B 678 56.070 9.447 67.831 1.00 28.29 B ATOM 4104 O THR B 678 54.934 9.742 68.215 1.00 29.19 B ATOM 4105 N PHE B 679 56.889 10.273 67.194 1.00 27.12 B ATOM 4106 CA PHE B 679 56.552 11.621 66.835 1.00 24.71 B ATOM 4107 CB PHE B 679 56.246 12.453 68.085 1.00 25.37 B ATOM 4108 CG PHE B 679 57.481 12.945 68.829 1.00 24.77 B ATOM 4109 CD1 PHE B 679 58.206 14.061 68.374 1.00 21.98 B ATOM 4110 CD2 PHE B 679 57.916 12.293 69.990 1.00 24.36 B ATOM 4111 CE1 PHE B 679 59.331 14.509 69.063 1.00 19.92 B ATOM 4112 CE2 PHE B 679 59.032 12.736 70.671 1.00 22.18 B ATOM 4113 CZ PHE B 679 59.739 13.845 70.207 1.00 21.94 B ATOM 4114 C PHE B 679 57.762 12.174 66.095 1.00 24.89 B ATOM 4115 O PHE B 679 58.894 11.669 66.212 1.00 21.91 B ATOM 4116 N TYR B 680 57.504 13.231 65.338 1.00 25.98 B ATOM 4117 CA TYR B 680 58.516 13.918 64.557 1.00 25.00 B ATOM 4118 CB TYR B 680 58.418 13.438 63.104 1.00 23.81 B ATOM 4119 CG TYR B 680 59.668 13.711 62.317 1.00 27.68 B ATOM 4120 CD1 TYR B 680 60.795 12.881 62.429 1.00 26.50 B ATOM 4121 CE1 TYR B 680 62.003 13.232 61.812 1.00 27.92 B ATOM 4122 CD2 TYR B 680 59.780 14.881 61.559 1.00 28.23 B ATOM 4123 CE2 TYR B 680 60.971 15.237 60.949 1.00 27.91 B ATOM 4124 CZ TYR B 680 62.074 14.427 61.080 1.00 28.40 B ATOM 4125 OH TYR B 680 63.253 14.870 60.531 1.00 31.86 B ATOM 4126 C TYR B 680 58.122 15.405 64.735 1.00 23.73 B ATOM 4127 O TYR B 680 56.975 15.684 65.090 1.00 22.88 B ATOM 4128 N VAL B 681 59.053 16.340 64.520 1.00 23.01 B ATOM 4129 CA VAL B 681 58.785 17.781 64.698 1.00 21.87 B ATOM 4130 CB VAL B 681 59.211 18.315 66.071 1.00 20.14 B ATOM 4131 CG1 VAL B 681 58.030 18.505 66.979 1.00 18.83 B ATOM 4132 CG2 VAL B 681 60.254 17.397 66.641 1.00 21.44 B ATOM 4133 C VAL B 681 59.556 18.695 63.781 1.00 21.58 B ATOM 4134 O VAL B 681 60.694 18.427 63.399 1.00 19.29 B ATOM 4135 N SER 8 682 58.928 19.818 63.480 1.00 21.27 B ATOM 4136 CA SER B 682 59.554 20.864 62.685 1.00 20.48 B ATOM 4137 CB SER B 682 58.923 20.956 61.300 1.00 19.96 B ATOM 4138 OG SER B 682 57.535 21.230 61.396 1.00 20.38 B ATOM 4139 C SER B 682 59.174 22.065 63.518 1.00 20.44 B ATOM 4140 O SER B 682 58.332 21.944 64.407 1.00 22.67 B ATOM 4141 N ASP B 683 59.797 23.207 63.275 1.00 19.98 B ATOM 4142 CA ASP B 683 59.441 24.394 64.036 1.00 19.73 B ATOM 4143 CB ASP B 683 60.212 25.638 63.547 1.00 20.26 B ATOM 4144 CG ASP B 683 61.708 25.650 63.959 1.00 21.54 B ATOM 4145 OD1 ASP B 683 62.132 24.891 64.860 1.00 19.41 B ATOM 4146 OD2 ASP B 683 62.468 26.460 63.377 1.00 22.23 B ATOM 4147 C ASP B 683 57.936 24.665 63.889 1.00 18.98 B ATOM 4148 O ASP B 683 57.351 25.254 64.782 1.00 19.03 B ATOM 4149 N ASN B 684 57.311 24.214 62.800 1.00 18.67 B ATOM 4150 CA ASN B 684 55.888 24.482 62.579 1.00 20.77 B ATOM 4151 CB ASN B 684 55.644 24.891 61.136 1.00 20.60 B ATOM 4152 CG ASN B 684 56.303 26.196 60.780 1.00 23.83 B ATOM 4153 OD1 ASN B 684 56.062 27.233 61.419 1.00 24.57 B ATOM 4154 ND2 ASN B 684 57.134 26.165 59.741 1.00 23.71 B ATOM 4155 C ASN B 684 54.874 23.392 62.886 1.00 22.90 B ATOM 4156 O ASN B 684 53.687 23.690 63.077 1.00 22.24 B ATOM 4157 N ILE B 685 55.327 22.140 62.890 1.00 23.24 B ATOM 4158 CA ILE B 685 54.449 20.997 63.118 1.00 20.82 B ATOM 4159 CB ILE B 685 54.156 20.257 61.778 1.00 19.24 B ATOM 4160 CG2 ILE B 685 53.256 19.057 62.014 1.00 18.99 B ATOM 4161 CG1 ILE B 685 53.488 21.211 60.784 1.00 17.58 B ATOM 4162 CD1 ILE B 685 52.067 21.562 61.120 1.00 17.99 B ATOM 4163 C ILE B 685 55.037 19.993 64.100 1.00 21.40 B ATOM 4164 O ILE B 685 56.263 19.961 64.315 1.00 21.31 B ATOM 4165 N LEU B 686 54.137 19.207 64.697 1.00 20.50 B ATOM 4166 CA LEU B 686 54.461 18.147 65.648 1.00 21.98 B ATOM 4167 CB LEU B 686 54.273 18.612 67.108 1.00 23.37 B ATOM 4168 CG LEU B 686 54.138 17.518 68.189 1.00 24.30 B ATOM 4169 CD1 LEU B 686 55.479 16.866 68.430 1.00 24.15 B ATOM 4170 CD2 LEU B 686 53.595 18.098 69.475 1.00 22.84 B ATOM 4171 C LEU B 686 53.475 17.026 65.361 1.00 22.92 B ATOM 4172 O LEU B 686 52.297 17.167 65.650 1.00 25.29 B ATOM 4173 N VAL B 687 53.927 15.924 64.780 1.00 21.99 B ATOM 4174 CA VAL B 687 53.018 14.817 64.511 1.00 21.64 B ATOM 4175 CB VAL B 687 53.186 14.346 63.000 1.00 22.41 B ATOM 4176 CG1 VAL B 687 52.604 12.949 62.796 1.00 21.78 B ATOM 4177 CG2 VAL B 687 52.476 15.325 62.052 1.00 19.88 B ATOM 4178 C VAL B 687 53.345 13.700 65.542 1.00 21.43 B ATOM 4179 O VAL B 687 54.476 13.202 65.599 1.00 21.65 B ATOM 4180 N SER B 688 52.387 13.330 66.390 1.00 21.20 B ATOM 4181 CA SER B 688 52.654 12.302 67.412 1.00 21.07 B ATOM 4182 CB SER B 688 52.601 12.920 68.812 1.00 21.19 B ATOM 4183 OG SER B 688 51.336 13.509 69.074 1.00 19.67 B ATOM 4184 C SER B 688 51.706 11.118 67.373 1.00 21.57 B ATOM 4185 O SER B 688 50.511 11.265 67.104 1.00 21.58 B ATOM 4186 N GLY B 689 52.221 9.935 67.674 1.00 23.31 B ATOM 4187 CA GLY B 689 51.348 8.778 67.635 1.00 25.20 B ATOM 4188 C GLY B 689 51.498 7.793 68.779 1.00 26.22 B ATOM 4189 O GLY B 689 52.590 7.549 69.295 1.00 26.74 B ATOM 4190 N SER B 690 50.372 7.245 69.200 1.00 26.47 B ATOM 4191 CA SER B 690 50.350 6.247 70.253 1.00 29.04 B ATOM 4192 CB SER B 690 49.977 6.881 71.601 1.00 30.51 B ATOM 4193 OG SER B 690 48.577 7.150 71.674 1.00 31.85 B ATOM 4194 C SER B 690 49.261 5.262 69.818 1.00 29.64 B ATOM 4195 O SER B 690 48.624 5.462 68.788 1.00 31.71 B ATOM 4196 N GLU B 691 49.037 4.213 70.599 1.00 29.52 B ATOM 4197 CA GLU B 691 48.005 3.239 70.280 1.00 28.36 B ATOM 4198 CB GLU B 691 47.857 2.282 71.452 1.00 28.07 B ATOM 4199 CG GLU B 691 46.563 1.512 71.496 1.00 32.75 B ATOM 4200 CD GLU B 691 46.531 0.499 72.635 1.00 35.90 B ATOM 4201 OE1 GLU B 691 47.285 −0.507 72.575 1.00 37.07 B ATOM 4202 OE2 GLU B 691 45.751 0.712 73.594 1.00 36.72 B ATOM 4203 C GLU B 691 46.689 3.970 70.013 1.00 27.98 B ATOM 4204 O GLU B 691 46.356 4.921 70.713 1.00 29.12 B ATOM 4205 N ASN B 692 45.968 3.554 68.974 1.00 27.34 B ATOM 4206 CA ASN B 692 44.678 4.159 68.617 1.00 27.55 B ATOM 4207 CB ASN B 692 43.625 3.832 69.671 1.00 30.51 B ATOM 4208 CG ASN B 692 43.363 2.347 69.797 1.00 33.53 B ATOM 4209 OD1 ASN B 692 42.997 1.866 70.874 1.00 34.93 B ATOM 4210 ND2 ASN B 692 43.537 1.607 68.694 1.00 36.41 B ATOM 4211 C ASN B 692 44.671 5.671 68.417 1.00 28.06 B ATOM 4212 O ASN B 692 43.611 6.271 68.227 1.00 27.85 B ATOM 4213 N GLN B 693 45.836 6.300 68.455 1.00 27.40 B ATOM 4214 CA GLN B 693 45.883 7.737 68.270 1.00 26.47 B ATOM 4215 CB GLN B 693 46.046 8.410 69.627 1.00 26.45 B ATOM 4216 CG GLN B 693 44.860 8.235 70.547 1.00 27.10 B ATOM 4217 CD GLN B 693 44.499 9.523 71.245 1.00 27.21 B ATOM 4218 OE1 GLN B 693 45.360 10.211 71.776 1.00 28.92 B ATOM 4219 NE2 GLN B 693 43.224 9.859 71.243 1.00 29.30 B ATOM 4220 C GLN B 693 46.999 8.200 67.320 1.00 26.29 B ATOM 4221 O GLN B 693 48.105 7.655 67.332 1.00 27.55 B ATOM 4222 N PHE B 694 46.700 9.196 66.487 1.00 24.60 B ATOM 4223 CA PHE B 694 47.675 9.771 65.551 1.00 22.51 B ATOM 4224 CB PHE B 694 47.612 9.073 64.184 1.00 20.48 B ATOM 4225 CG PHE B 694 48.701 9.499 63.210 1.00 20.42 B ATOM 4226 CD1 PHE B 694 49.967 8.922 63.241 1.00 20.85 B ATOM 4227 CD2 PHE B 694 48.441 10.465 62.237 1.00 21.71 B ATOM 4228 CE1 PHE B 694 50.956 9.301 62.312 1.00 21.35 B ATOM 4229 CE2 PHE B 694 49.421 10.851 61.304 1.00 20.94 B ATOM 4230 CZ PHE B 694 50.674 10.269 61.343 1.00 20.97 B ATOM 4231 C PHE B 694 47.234 11.227 65.445 1.00 22.04 B ATOM 4232 O PHE B 694 46.146 11.508 64.951 1.00 22.64 B ATOM 4233 N ASN B 695 48.065 12.142 65.947 1.00 22.40 B ATOM 4234 CA ASN B 695 47.741 13.570 65.946 1.00 22.71 B ATOM 4235 CB ASN B 695 47.542 14.102 67.383 1.00 24.16 B ATOM 4236 CG ASN B 695 46.687 13.194 68.246 1.00 27.03 B ATOM 4237 OD1 ASN B 695 47.145 12.735 69.297 1.00 30.17 B ATOM 4238 ND2 ASN B 695 45.441 12.930 67.817 1.00 28.07 B ATOM 4239 C ASN B 695 48.762 14.477 65.261 1.00 21.75 B ATOM 4240 O ASN B 695 49.960 14.194 65.232 1.00 20.80 B ATOM 4241 N ILE B 696 48.248 15.588 64.734 1.00 21.52 B ATOM 4242 CA ILE B 696 49.024 16.622 64.045 1.00 20.16 B ATOM 4243 CB ILE B 696 48.592 16.711 62.556 1.00 17.92 B ATOM 4244 CG2 ILE B 696 49.367 17.768 61.821 1.00 16.21 B ATOM 4245 CG1 ILE B 696 48.860 15.371 61.883 1.00 16.96 B ATOM 4246 CD1 ILE B 696 48.335 15.277 60.471 1.00 14.78 B ATOM 4247 C ILE B 696 48.732 17.922 64.803 1.00 20.71 B ATOM 4248 O ILE B 696 47.589 18.207 65.167 1.00 20.57 B ATOM 4249 N TYR B 697 49.779 18.690 65.057 1.00 21.04 B ATOM 4250 CA TYR B 697 49.651 19.916 65.816 1.00 22.01 B ATOM 4251 CB TYR B 697 50.334 19.746 67.174 1.00 22.18 B ATOM 4252 CG TYR B 697 49.748 18.654 68.027 1.00 22.67 B ATOM 4253 CD1 TYR B 697 48.702 18.919 68.917 1.00 21.46 B ATOM 4254 CE1 TYR B 697 48.167 17.910 69.717 1.00 20.34 B ATOM 4255 CD2 TYR B 697 50.244 17.349 67.952 1.00 22.41 B ATOM 4256 CE2 TYR B 697 49.717 16.331 68.746 1.00 22.87 B ATOM 4257 CZ TYR B 697 48.685 16.615 69.627 1.00 21.85 B ATOM 4258 OH TYR B 697 48.212 15.607 70.431 1.00 22.33 B ATOM 4259 C TYR B 697 50.244 21.121 65.112 1.00 23.61 B ATOM 4260 O TYR B 697 51.334 21.080 64.538 1.00 25.65 B ATOM 4261 N ASN B 698 49.491 22.202 65.162 1.00 23.81 B ATOM 4262 CA ASN B 698 49.913 23.449 64.594 1.00 23.42 B ATOM 4263 CB ASN B 698 48.680 24.254 64.224 1.00 26.51 B ATOM 4264 CG ASN B 698 49.020 25.531 63.512 1.00 28.61 B ATOM 4265 OD1 ASN B 698 49.959 26.238 63.897 1.00 28.06 B ATOM 4266 ND2 ASN B 698 48.255 25.849 62.472 1.00 29.88 B ATOM 4267 C ASN B 698 50.658 24.079 65.778 1.00 23.71 B ATOM 4268 O ASN B 698 50.047 24.586 66.726 1.00 22.24 B ATOM 4269 N LEU B 699 51.980 23.982 65.732 1.00 23.60 B ATOM 4270 CA LEU B 699 52.841 24.497 66.773 1.00 24.06 B ATOM 4271 CB LEU B 699 54.270 24.037 66.517 1.00 22.91 B ATOM 4272 CG LEU B 699 54.837 22.996 67.475 1.00 23.91 B ATOM 4273 CD1 LEU B 699 53.784 21.972 67.874 1.00 24.32 B ATOM 4274 CD2 LEU B 699 56.028 22.362 66.832 1.00 22.79 B ATOM 4275 C LEU B 699 52.801 26.001 66.862 1.00 25.53 B ATOM 4276 O LEU B 699 53.498 26.580 67.681 1.00 27.08 B ATOM 4277 N ARG B 700 52.004 26.631 66.002 1.00 26.51 B ATOM 4278 CA ARG B 700 51.863 28.087 65.997 1.00 25.40 B ATOM 4279 CB ARG B 700 51.489 28.600 64.609 1.00 27.54 B ATOM 4280 CG ARG B 700 52.549 28.502 63.543 1.00 28.72 B ATOM 4281 CD ARG B 700 53.706 29.422 63.820 1.00 31.33 B ATOM 4282 NE ARG B 700 54.598 29.480 62.671 1.00 34.27 B ATOM 4283 CZ ARG B 700 54.233 29.908 61.464 1.00 36.22 B ATOM 4284 NH1 ARG B 700 52.989 30.318 61.259 1.00 35.49 B ATOM 4285 NH2 ARG B 700 55.107 29.920 60.457 1.00 38.36 B ATOM 4286 C ARG B 700 50.724 28.431 66.942 1.00 24.24 B ATOM 4287 O ARG B 700 50.914 29.118 67.928 1.00 22.77 B ATOM 4288 N SER B 701 49.532 27.949 66.620 1.00 23.91 B ATOM 4289 CA SER B 701 48.358 28.202 67.435 1.00 23.69 B ATOM 4290 CB SER B 701 47.105 27.928 66.633 1.00 21.95 B ATOM 4291 OG SER B 701 47.096 26.574 66.220 1.00 21.41 B ATOM 4292 C SER B 701 48.342 27.281 68.627 1.00 25.56 B ATOM 4293 O SER B 701 47.546 27.467 69.541 1.00 27.95 B ATOM 4294 N GLY B 702 49.207 26.273 68.606 1.00 25.80 B ATOM 4295 CA GLY B 702 49.252 25.311 69.688 1.00 25.16 B ATOM 4296 C GLY B 702 48.080 24.351 69.601 1.00 25.57 B ATOM 4297 O GLY B 702 47.963 23.464 70.427 1.00 27.20 B ATOM 4298 N LYS B 703 47.221 24.498 68.597 1.00 26.86 B ATOM 4299 CA LYS B 703 46.049 23.630 68.485 1.00 29.85 B ATOM 4300 CB LYS B 703 44.846 24.452 67.982 1.00 31.50 B ATOM 4301 CG LYS B 703 44.521 25.679 68.857 1.00 35.32 B ATOM 4302 CD LYS B 703 43.066 26.160 68.704 1.00 35.78 B ATOM 4303 CE LYS B 703 42.529 26.768 70.007 1.00 39.24 B ATOM 4304 NZ LYS B 703 42.643 25.841 71.218 1.00 39.02 B ATOM 4305 C LYS B 703 46.199 22.357 67.631 1.00 29.87 B ATOM 4306 O LYS B 703 47.079 22.245 66.786 1.00 31.67 B ATOM 4307 N LEU B 704 45.314 21.403 67.868 1.00 29.38 B ATOM 4308 CA LEU B 704 45.319 20.152 67.149 1.00 29.31 B ATOM 4309 CB LEU B 704 44.445 19.169 67.892 1.00 28.56 B ATOM 4310 CG LEU B 704 44.409 17.731 67.419 1.00 29.17 B ATOM 4311 CD1 LEU B 704 45.768 17.030 67.620 1.00 29.83 B ATOM 4312 CD2 LEU B 704 43.340 17.041 68.206 1.00 28.68 B ATOM 4313 C LEU B 704 44.732 20.390 65.772 1.00 30.18 B ATOM 4314 O LEU B 704 43.610 20.880 65.669 1.00 32.27 B ATOM 4315 N VAL B 705 45.458 20.053 64.709 1.00 30.79 B ATOM 4316 CA VAL B 705 44.908 20.275 63.371 1.00 31.43 B ATOM 4317 CB VAL B 705 46.012 20.551 62.322 1.00 30.01 B ATOM 4318 CG1 VAL B 705 45.368 20.883 60.976 1.00 28.32 B ATOM 4319 CG2 VAL B 705 46.889 21.685 62.776 1.00 29.54 B ATOM 4320 C VAL B 705 44.069 19.087 62.904 1.00 32.61 B ATOM 4321 O VAL B 705 42.930 19.252 62.462 1.00 32.10 B ATOM 4322 N HIS B 706 44.641 17.890 63.003 1.00 35.60 B ATOM 4323 CA HIS B 706 43.949 16.665 62.613 1.00 37.51 B ATOM 4324 CB HIS B 706 44.515 16.131 61.302 1.00 40.51 B ATOM 4325 CG HIS B 706 44.191 16.972 60.110 1.00 43.09 B ATOM 4326 CD2 HIS B 706 44.947 17.845 59.402 1.00 44.48 B ATOM 4327 ND1 HIS B 706 42.946 16.973 59.521 1.00 43.58 B ATOM 4328 CE1 HIS B 706 42.948 17.814 58.501 1.00 44.83 B ATOM 4329 NE2 HIS B 706 44.149 18.357 58.407 1.00 45.93 B ATOM 4330 C HIS B 706 44.109 15.583 63.676 1.00 37.67 B ATOM 4331 O HIS B 706 45.189 15.396 64.267 1.00 38.10 B ATOM 4332 N ALA B 707 43.032 14.852 63.917 1.00 37.33 B ATOM 4333 CA ALA B 707 43.104 13.773 64.891 1.00 35.31 B ATOM 4334 CB ALA B 707 42.368 14.163 66.163 1.00 33.61 B ATOM 4335 C ALA B 707 42.540 12.479 64.322 1.00 33.93 B ATOM 4336 O ALA B 707 42.616 11.455 64.979 1.00 33.97 B ATOM 4337 N ASN B 708 42.000 12.508 63.103 1.00 32.93 B ATOM 4338 CA ASN B 708 41.438 11.278 62.566 1.00 32.08 B ATOM 4339 CB ASN B 708 39.900 11.381 62.527 1.00 30.21 B ATOM 4340 CG ASN B 708 39.282 11.431 63.935 1.00 29.73 B ATOM 4341 OD1 ASN B 708 39.641 10.644 64.808 1.00 32.17 B ATOM 4342 ND2 ASN B 708 38.369 12.355 64.155 1.00 27.91 B ATOM 4343 C ASN B 708 41.998 10.810 61.227 1.00 31.64 B ATOM 4344 O ASN B 708 41.468 9.888 60.605 1.00 30.96 B ATOM 4345 N ILE B 709 43.104 11.412 60.803 1.00 31.19 B ATOM 4346 CA ILE B 709 43.709 11.050 59.526 1.00 29.76 B ATOM 4347 CB ILE B 709 45.027 11.813 59.279 1.00 30.79 B ATOM 4348 CG2 ILE B 709 45.414 11.698 57.830 1.00 30.87 B ATOM 4349 CG1 ILE B 709 44.846 13.292 59.585 1.00 31.89 B ATOM 4350 CD1 ILE B 709 43.831 13.966 58.690 1.00 33.84 B ATOM 4351 C ILE B 709 43.992 9.554 59.404 1.00 27.56 B ATOM 4352 O ILE B 709 43.923 9.003 58.316 1.00 28.85 B ATOM 4353 N LEU B 710 44.335 8.892 60.498 1.00 24.88 B ATOM 4354 CA LEU B 710 44.600 7.464 60.406 1.00 23.14 B ATOM 4355 CB LEU B 710 46.101 7.207 60.581 1.00 19.23 B ATOM 4356 CG LEU B 710 47.171 7.770 59.617 1.00 17.21 B ATOM 4357 CD1 LEU B 710 48.565 7.336 60.119 1.00 12.65 B ATOM 4358 CD2 LEU B 710 46.952 7.271 58.159 1.00 11.32 B ATOM 4359 C LEU B 710 43.787 6.738 61.491 1.00 24.82 B ATOM 4360 O LEU B 710 44.278 5.820 62.165 1.00 26.12 B ATOM 4361 N LYS B 711 42.540 7.172 61.668 1.00 24.22 B ATOM 4362 CA LYS B 711 41.672 6.583 62.678 1.00 23.87 B ATOM 4363 CB LYS B 711 40.223 7.113 62.551 1.00 23.07 B ATOM 4364 CG LYS B 711 39.704 7.286 61.127 0.00 24.07 B ATOM 4365 CD LYS B 711 39.138 6.000 60.567 0.00 24.51 B ATOM 4366 CE LYS B 711 38.815 6.171 59.096 0.00 24.91 B ATOM 4367 NZ LYS B 711 38.073 5.005 58.557 0.00 25.25 B ATOM 4368 C LYS B 711 41.697 5.066 62.640 1.00 22.54 B ATOM 4369 O LYS B 711 41.789 4.435 63.682 1.00 21.78 B ATOM 4370 N ASP B 712 41.656 4.474 61.450 1.00 24.59 B ATOM 4371 CA ASP B 712 41.649 3.009 61.346 1.00 26.66 B ATOM 4372 CB ASP B 712 41.358 2.577 59.902 1.00 27.40 B ATOM 4373 CG ASP B 712 42.533 2.779 58.971 1.00 29.97 B ATOM 4374 OD1 ASP B 712 43.376 3.660 59.238 1.00 31.04 B ATOM 4375 OD2 ASP B 712 42.601 2.059 57.945 1.00 32.95 B ATOM 4376 C ASP B 712 42.908 2.320 61.846 1.00 27.18 B ATOM 4377 O ASP B 712 42.933 1.100 61.992 1.00 28.41 B ATOM 4378 N ALA B 713 43.943 3.099 62.131 1.00 26.51 B ATOM 4379 CA ALA B 713 45.192 2.526 62.600 1.00 27.91 B ATOM 4380 CB ALA B 713 46.334 3.505 62.337 1.00 25.17 B ATOM 4381 C ALA B 713 45.117 2.185 64.091 1.00 29.57 B ATOM 4382 O ALA B 713 44.650 3.003 64.889 1.00 30.09 B ATOM 4383 N ASP B 714 45.584 0.991 64.467 1.00 30.92 B ATOM 4384 CA ASP B 714 45.568 0.564 65.873 1.00 33.02 B ATOM 4385 CB ASP B 714 45.300 −0.947 65.975 1.00 34.69 B ATOM 4386 CG ASP B 714 43.997 −1.348 65.333 1.00 36.43 B ATOM 4387 OD1 ASP B 714 42.933 −0.920 65.810 1.00 38.16 B ATOM 4388 OD2 ASP B 714 44.033 −2.089 64.337 1.00 40.68 B ATOM 4389 C ASP B 714 46.871 0.908 66.620 1.00 33.35 B ATOM 4390 O ASP B 714 46.871 1.124 67.837 1.00 33.65 B ATOM 4391 N GLN B 715 47.979 0.948 65.888 1.00 32.50 B ATOM 4392 CA GLN B 715 49.272 1.292 66.470 1.00 31.33 B ATOM 4393 CB GLN B 715 50.053 0.028 66.851 1.00 32.90 B ATOM 4394 CG GLN B 715 49.555 −0.657 68.107 1.00 36.42 B ATOM 4395 CD GLN B 715 49.806 0.172 69.355 1.00 39.19 B ATOM 4396 OE1 GLN B 715 49.528 −0.273 70.465 1.00 39.45 B ATOM 4397 NE2 GLN B 715 50.342 1.389 69.175 1.00 41.12 B ATOM 4398 CG LN B 715 50.063 2.123 65.465 1.00 29.87 B ATOM 4399 O GLN B 715 49.897 1.967 64.254 1.00 28.89 B ATOM 4400 N ILE B 716 50.885 3.038 65.968 1.00 28.35 B ATOM 4401 CA ILE B 716 51.712 3.875 65.102 1.00 26.58 B ATOM 4402 CB ILE B 716 51.360 5.388 65.216 1.00 26.71 B ATOM 4403 CG2 ILE B 716 52.387 6.226 64.452 1.00 24.23 B ATOM 4404 CG1 ILE B 716 49.979 5.655 64.611 1.00 27.09 B ATOM 4405 CD1 ILE B 716 48.830 5.042 65.381 1.00 29.06 B ATOM 4406 C ILE B 716 53.137 3.644 65.567 1.00 26.24 B ATOM 4407 O ILE B 716 53.563 4.184 66.583 1.00 25.69 B ATOM 4408 N TRP B 717 53.870 2.833 64.818 1.00 25.09 B ATOM 4409 CA TRP B 717 55.219 2.505 65.198 1.00 25.49 B ATOM 4410 CB TRP B 717 55.658 1.210 64.497 1.00 28.30 B ATOM 4411 CG TRP B 717 54.780 0.010 64.877 1.00 31.04 B ATOM 4412 CD2 TRP B 717 54.454 −0.438 66.203 1.00 29.45 B ATOM 4413 CE2 TRP B 717 53.559 −1.521 66.071 1.00 29.85 B ATOM 4414 CE3 TRP B 717 54.828 −0.029 67.483 1.00 30.32 B ATOM 4415 CD1 TRP B 717 54.091 −0.807 64.024 1.00 30.88 B ATOM 4416 NE1 TRP B 717 53.353 −1.724 64.736 1.00 29.32 B ATOM 4417 CZ2 TRP B 717 53.027 −2.199 67.172 1.00 33.01 B ATOM 4418 CZ3 TRP B 717 54.295 −0.706 68.583 1.00 33.00 B ATOM 4419 CH2 TRP B 717 53.406 −1.778 68.416 1.00 32.26 B ATOM 4420 C TRP B 717 56.207 3.611 64.925 1.00 25.13 B ATOM 4421 O TRP B 717 56.995 3.961 65.782 1.00 27.18 B ATOM 4422 N SER B 718 56.163 4.189 63.743 1.00 24.84 B ATOM 4423 CA SER B 718 57.127 5.212 63.423 1.00 24.34 B ATOM 4424 CB SER B 718 58.314 4.536 62.727 1.00 24.77 B ATOM 4425 OG SER B 718 59.315 5.464 62.352 1.00 29.36 B ATOM 4426 C SER B 718 56.477 6.265 62.533 1.00 23.95 B ATOM 4427 O SER B 718 55.668 5.949 61.663 1.00 24.34 B ATOM 4428 N VAL B 719 56.813 7.521 62.754 1.00 21.34 B ATOM 4429 CA VAL B 719 56.236 8.549 61.934 1.00 20.74 B ATOM 4430 CB VAL B 719 55.041 9.202 62.663 1.00 20.34 B ATOM 4431 CG1 VAL B 719 55.531 10.069 63.799 1.00 20.79 B ATOM 4432 CG2 VAL B 719 54.182 9.964 61.685 1.00 20.98 B ATOM 4433 C VAL B 719 57.355 9.538 61.608 1.00 21.48 B ATOM 4434 O VAL B 719 58.204 9.840 62.452 1.00 21.37 B ATOM 4435 N ASN B 720 57.391 10.001 60.368 1.00 20.75 B ATOM 4436 CA ASN B 720 58.434 10.915 59.950 1.00 20.33 B ATOM 4437 CB ASN B 720 59.582 10.130 59.331 1.00 19.95 B ATOM 4438 CG ASN B 720 60.744 11.013 58.939 1.00 20.71 B ATOM 4439 OD1 ASN B 720 60.570 12.186 58.613 1.00 22.75 B ATOM 4440 ND2 ASN B 720 61.934 10.452 58.960 1.00 19.81 B ATOM 4441 C ASN B 720 57.831 11.792 58.885 1.00 21.17 B ATOM 4442 O ASN B 720 57.037 11.318 58.078 1.00 23.00 B ATOM 4443 N PHE B 721 58.187 13.067 58.850 1.00 20.66 B ATOM 4444 CA PHE B 721 57.630 13.907 57.791 1.00 21.75 B ATOM 4445 CB PHE B 721 56.339 14.591 58.289 1.00 17.46 B ATOM 4446 CG PHE B 721 56.556 15.653 59.312 1.00 14.32 B ATOM 4447 CO1 PHE B 721 56.870 16.939 58.921 1.00 10.85 B ATOM 4448 CD2 PHE B 721 56.404 15.387 60.660 1.00 11.84 B ATOM 4449 CE1 PHE B 721 57.028 17.953 59.855 1.00 10.06 B ATOM 4450 CE2 PHE B 721 56.561 16.405 61.607 1.00 13.14 B ATOM 4451 CZ PHE B 721 56.873 17.693 61.198 1.00 12.02 B ATOM 4452 C PHE B 721 58.656 14.902 57.259 1.00 22.48 B ATOM 4453 O PHE B 721 59.528 15.344 58.000 1.00 21.67 B ATOM 4454 N LYS B 722 58.584 15.205 55.961 1.00 24.01 B ATOM 4455 CA LYS B 722 59.508 16.161 55.320 1.00 24.93 B ATOM 4456 CB LYS B 722 60.752 15.450 54.783 1.00 25.59 B ATOM 4457 CG LYS B 722 61.838 15.134 55.800 1.00 27.22 B ATOM 4458 CD LYS B 722 62.834 16.283 55.958 0.00 27.08 B ATOM 4459 CE LYS B 722 62.210 17.519 56.576 0.00 27.46 B ATOM 4460 NZ LYS B 722 63.225 18.601 56.697 0.00 27.62 B ATOM 4461 C LYS B 722 58.838 16.863 54.151 1.00 24.47 B ATOM 4462 O LYS B 722 58.571 16.242 53.121 1.00 25.21 B ATOM 4463 N GLY B 723 58.569 18.153 54.298 1.00 24.23 B ATOM 4464 CA GLY B 723 57.937 18.872 53.209 1.00 26.31 B ATOM 4465 C GLY B 723 56.464 18.536 53.019 1.00 28.74 B ATOM 4466 O GLY B 723 55.694 18.529 53.979 1.00 29.75 B ATOM 4467 N LYS B 724 56.057 18.235 51.794 1.00 28.84 B ATOM 4468 CA LYS B 724 54.652 17.941 51.530 1.00 29.80 B ATOM 4469 CB LYS B 724 54.352 18.219 50.074 1.00 31.52 B ATOM 4470 CG LYS B 724 55.436 17.698 49.171 1.00 32.34 B ATOM 4471 CD LYS B 724 54.881 16.783 48.115 1.00 33.78 B ATOM 4472 CE LYS B 724 55.974 16.447 47.107 1.00 35.08 B ATOM 4473 NZ LYS B 724 56.379 17.659 46.344 1.00 33.47 B ATOM 4474 C LYS B 724 54.184 16.535 51.841 1.00 29.68 B ATOM 4475 O LYS B 724 52.988 16.260 51.801 1.00 28.58 B ATOM 4476 N THR B 725 55.121 15.643 52.135 1.00 29.01 B ATOM 4477 CA THR B 725 54.768 14.261 52.412 1.00 28.07 B ATOM 4478 CB THR B 725 55.459 13.315 51.372 1.00 28.24 B ATOM 4479 OG1 THR B 725 55.740 12.040 51.957 1.00 28.44 B ATOM 4480 CG2 THR B 725 56.732 13.943 50.850 1.00 29.05 B ATOM 4481 C THR B 725 55.081 13.853 53.847 1.00 27.60 B ATOM 4482 O THR B 725 56.070 14.292 54.445 1.00 27.85 B ATOM 4483 N LEU B 726 54.190 13.036 54.399 1.00 26.00 B ATOM 4484 CA LEU B 726 54.310 12.528 55.755 1.00 24.86 B ATOM 4485 CB LEU B 726 53.147 13.030 56.612 1.00 23.41 B ATOM 4486 CG LEU B 726 52.907 12.266 57.924 1.00 21.65 B ATOM 4487 OD1 LEU B 726 54.123 12.369 58.805 1.00 24.41 B ATOM 4488 CD2 LEU B 726 51.698 12.816 58.643 1.00 21.21 B ATOM 4489 C LEU B 726 54.254 11.014 55.677 1.00 25.90 B ATOM 4490 O LEU B 726 53.370 10.464 55.019 1.00 27.58 B ATOM 4491 N VAL B 727 55.196 10.329 56.315 1.00 24.78 B ATOM 4492 CA VAL B 727 55.151 8.875 56.283 1.00 25.06 B ATOM 4493 CB VAL B 727 56.388 8.256 55.556 1.00 23.86 B ATOM 4494 CG1 VAL B 727 56.432 8.730 54.129 1.00 22.56 B ATOM 4495 CG2 VAL B 727 57.678 8.571 56.296 1.00 23.51 B ATOM 4496 C VAL B 727 55.009 8.257 57.680 1.00 25.61 B ATOM 4497 O VAL B 727 55.637 8.717 58.641 1.00 25.40 B ATOM 4498 N ALA B 728 54.163 7.224 57.775 1.00 26.51 B ATOM 4499 CA ALA B 728 53.898 6.501 59.028 1.00 27.01 B ATOM 4500 CB ALA B 728 52.656 7.087 59.692 1.00 25.86 B ATOM 4501 C ALA B 728 53.734 4.960 58.886 1.00 27.72 B ATOM 4502 O ALA B 728 52.981 4.480 58.039 1.00 28.25 B ATOM 4503 N ALA B 729 54.457 4.204 59.718 1.00 29.53 B ATOM 4504 CA ALA B 729 54.401 2.735 59.745 1.00 30.38 B ATOM 4505 CB ALA B 729 55.761 2.150 60.042 1.00 26.88 B ATOM 4506 C ALA B 729 53.441 2.404 60.876 1.00 32.48 B ATOM 4507 O ALA B 729 53.692 2.754 62.036 1.00 32.95 B ATOM 4508 N VAL B 730 52.358 1.710 60.541 1.00 34.76 B ATOM 4509 CA VAL B 730 51.326 1.409 61.520 1.00 36.48 B ATOM 4510 CB VAL B 730 50.133 2.339 61.277 1.00 35.80 B ATOM 4511 CG1 VAL B 730 50.546 3.802 61.484 1.00 35.67 B ATOM 4512 CG2 VAL B 730 49.642 2.148 59.859 1.00 35.12 B ATOM 4513 C VAL B 730 50.819 −0.022 61.471 1.00 37.73 B ATOM 4514 O VAL B 730 51.069 −0.738 60.507 1.00 39.94 B ATOM 4515 N GLU B 731 50.102 −0.422 62.520 1.00 38.43 B ATOM 4516 CA GLU B 731 49.509 −1.755 62.608 1.00 38.21 B ATOM 4517 CB GLU B 731 49.851 −2.413 63.929 1.00 37.52 B ATOM 4518 CG GLU B 731 49.515 −3.869 63.933 1.00 39.46 B ATOM 4519 CD GLU B 731 49.255 −4.398 65.328 1.00 41.40 B ATOM 4520 OE1 GLU B 731 48.163 −4.105 65.873 1.00 41.33 B ATOM 4521 OE2 GLU B 731 50.140 −5.101 65.877 1.00 42.25 B ATOM 4522 C GLU B 731 47.996 −1.611 62.504 1.00 39.22 B ATOM 4523 O GLU B 731 47.393 −0.781 63.189 1.00 38.41 B ATOM 4524 N LYS B 732 47.382 −2.424 61.652 1.00 41.10 B ATOM 4525 CA LYS B 732 45.938 −2.358 61.449 1.00 43.00 B ATOM 4526 CB LYS B 732 45.635 −1.485 60.226 1.00 42.61 B ATOM 4527 CG LYS B 732 46.197 −0.077 60.333 0.00 43.37 B ATOM 4528 CD LYS B 732 46.607 0.492 58.981 0.00 43.64 B ATOM 4529 CE LYS B 732 45.431 0.678 58.036 0.00 43.89 B ATOM 4530 NZ LYS B 732 45.868 1.358 56.783 0.00 44.01 B ATOM 4531 C LYS B 732 45.381 −3.753 61.237 1.00 44.67 B ATOM 4532 O LYS B 732 45.879 −4.500 60.393 1.00 45.72 B ATOM 4533 N ASP B 733 44.350 −4.100 62.004 1.00 46.86 B ATOM 4534 CA ASP B 733 43.717 −5.417 61.898 1.00 48.20 B ATOM 4535 CB ASP B 733 43.098 −5.602 60.502 1.00 51.83 B ATOM 4536 CG ASP B 733 42.192 −6.824 60.411 1.00 54.62 B ATOM 4537 OD1 ASP B 733 42.658 −7.894 59.947 1.00 55.49 B ATOM 4538 OD2 ASP B 733 41.009 −6.708 60.812 1.00 55.81 B ATOM 4539 C ASP B 733 44.744 −6.520 62.159 1.00 46.65 B ATOM 4540 O ASP B 733 44.653 −7.621 61.614 1.00 46.27 B ATOM 4541 N GLY B 734 45.739 −6.203 62.977 1.00 45.55 B ATOM 4542 CA GLY B 734 46.749 −7.182 63.308 1.00 45.42 B ATOM 4543 C GLY B 734 47.792 −7.446 62.245 1.00 45.85 B ATOM 4544 O GLY B 734 48.334 −8.548 62.183 1.00 46.44 B ATOM 4545 N GLN B 735 48.073 −6.454 61.401 1.00 46.81 B ATOM 4546 CA GLN B 735 49.093 −6.599 60.355 1.00 47.05 B ATOM 4547 CB GLN B 735 48.461 −7.018 59.028 1.00 48.17 B ATOM 4548 CG GLN B 735 48.028 −8.461 59.027 1.00 52.88 B ATOM 4549 CD GLN B 735 46.961 −8.755 57.990 1.00 56.44 B ATOM 4550 OE1 GLN B 735 46.245 −9.766 58.087 1.00 58.95 B ATOM 4551 NE2 GLN B 735 46.840 −7.878 56.993 1.00 55.74 B ATOM 4552 C GLN B 735 49.897 −5.317 60.176 1.00 45.22 B ATOM 4553 O GLN B 735 49.597 −4.297 60.789 1.00 46.16 B ATOM 4554 N SER B 736 50.924 −5.394 59.336 1.00 42.48 B ATOM 4555 CA SER B 736 51.817 −4.278 59.061 1.00 39.38 B ATOM 4556 CB SER B 736 53.256 −4.791 59.003 1.00 40.16 B ATOM 4557 OG SER B 736 54.176 −3.797 59.394 1.00 40.72 B ATOM 4558 C SER B 736 51.468 −3.563 57.753 1.00 37.61 B ATOM 4559 O SER B 736 51.155 −4.193 56.734 1.00 37.66 B ATOM 4560 N PHE B 737 51.549 −2.239 57.797 1.00 33.84 B ATOM 4561 CA PHE B 737 51.228 −1.405 56.655 1.00 31.74 B ATOM 4562 CB PHE B 737 49.753 −1.006 56.716 1.00 32.02 B ATOM 4563 CG PHE B 737 48.802 −2.099 56.337 1.00 33.36 B ATOM 4564 CD1 PHE B 737 48.776 −2.582 55.041 1.00 34.70 B ATOM 4565 CD2 PHE B 737 47.894 −2.606 57.255 1.00 35.15 B ATOM 4566 CE1 PHE B 737 47.857 −3.545 54.655 1.00 36.59 B ATOM 4567 CE2 PHE B 737 46.964 −3.573 56.878 1.00 35.49 B ATOM 4568 CZ PHE B 737 46.946 −4.044 55.573 1.00 36.38 B ATOM 4569 C PHE B 737 52.077 −0.134 56.644 1.00 30.68 B ATOM 4570 O PHE B 737 52.650 0.254 57.665 1.00 31.62 B ATOM 4571 N LEU B 738 52.165 0.510 55.485 1.00 27.59 B ATOM 4572 CA LEU B 738 52.905 1.758 55.373 1.00 25.56 B ATOM 4573 CB LEU B 738 54.042 1.679 54.355 1.00 25.25 B ATOM 4574 CG LEU B 738 54.884 2.973 54.305 1.00 25.05 B ATOM 4575 CD1 LEU B 738 55.668 3.104 55.614 1.00 22.91 B ATOM 4576 CD2 LEU B 738 55.839 2.973 53.131 1.00 21.80 B ATOM 4577 C LEU B 738 51.947 2.841 54.922 1.00 24.87 B ATOM 4578 O LEU B 738 51.336 2.743 53.864 1.00 23.89 B ATOM 4579 N GLU B 739 51.820 3.882 55.728 1.00 24.71 B ATOM 4580 CA GLU B 739 50.940 4.976 55.372 1.00 23.29 B ATOM 4581 CB GLU B 739 50.206 5.458 56.612 1.00 24.09 B ATOM 4582 CG GLU B 739 48.692 5.452 56.495 1.00 28.17 B ATOM 4583 CD GLU B 739 48.058 4.066 56.517 1.00 28.62 B ATOM 4584 OE1 GLU B 739 48.352 3.273 57.426 1.00 31.20 B ATOM 4585 OE2 GLU B 739 47.232 3.782 55.633 1.00 28.53 B ATOM 4586 C GLU B 739 51.795 6.094 54.780 1.00 20.71 B ATOM 4587 O GLU B 739 52.906 6.329 55.235 1.00 20.52 B ATOM 4588 N ILE B 740 51.290 6.740 53.732 1.00 19.91 B ATOM 4589 CA ILE B 740 51.968 7.868 53.075 1.00 19.31 B ATOM 4590 CB ILE B 740 52.572 7.473 51.720 1.00 17.66 B ATOM 4591 CG2 ILE B 740 53.171 8.701 51.030 1.00 15.65 B ATOM 4592 CG1 ILE B 740 53.604 6.379 51.926 1.00 16.52 B ATOM 4593 CD1 ILE B 740 54.155 5.833 50.629 1.00 18.73 B ATOM 4594 C ILE B 740 50.891 8.923 52.849 1.00 19.07 B ATOM 4595 O ILE B 740 49.886 8.655 52.209 1.00 19.78 B ATOM 4596 N LEU B 741 51.106 10.111 53.395 1.00 19.72 B ATOM 4597 CA LEU B 741 50.151 11.188 53.259 1.00 21.30 B ATOM 4598 CB LEU B 741 49.728 11.648 54.645 1.00 22.07 B ATOM 4599 CG LEU B 741 49.077 10.572 55.530 1.00 23.25 B ATOM 4600 CD1 LEU B 741 48.660 11.188 56.855 1.00 23.41 B ATOM 4601 CD2 LEU B 741 47.856 9.989 54.825 1.00 23.48 B ATOM 4602 C LEU B 741 50.732 12.357 52.461 1.00 22.75 B ATOM 4603 O LEU B 741 51.891 12.745 52.656 1.00 24.38 B ATOM 4604 N ASP B 742 49.918 12.918 51.571 1.00 23.48 B ATOM 4605 CA ASP B 742 50.324 14.032 50.711 1.00 24.55 B ATOM 4606 CB ASP B 742 49.931 13.723 49.276 1.00 26.67 B ATOM 4607 CG ASP B 742 50.733 14.515 48.271 1.00 28.63 B ATOM 4608 OD1 ASP B 742 50.840 15.760 48.424 1.00 28.82 B ATOM 4609 OD2 ASP B 742 51.245 13.879 47.328 1.00 28.63 B ATOM 4610 C ASP B 742 49.688 15.363 51.103 1.00 25.06 B ATOM 4611 O ASP B 742 48.481 15.436 51.305 1.00 26.84 B ATOM 4612 N PHE B 743 50.484 16.423 51.183 1.00 25.71 B ATOM 4613 CA PHE B 743 49.943 17.731 51.558 1.00 27.52 B ATOM 4614 CB PHE B 743 50.486 18.191 52.912 1.00 26.16 B ATOM 4615 CG PHE B 743 49.997 17.388 54.073 1.00 24.94 B ATOM 4616 CD1 PHE B 743 50.565 16.158 54.378 1.00 24.17 B ATOM 4617 CD2 PHE B 743 48.980 17.887 54.890 1.00 23.91 B ATOM 4618 CE1 PHE B 743 50.132 15.437 55.490 1.00 24.90 B ATOM 4619 CE2 PHE B 743 48.537 17.184 56.000 1.00 21.83 B ATOM 4620 CZ PHE B 743 49.111 15.957 56.306 1.00 23.09 B ATOM 4621 C PHE B 743 50.249 18.808 50.530 1.00 29.26 B ATOM 4622 O PHE B 743 50.140 20.005 50.808 1.00 29.97 B ATOM 4623 N SER B 744 50.646 18.372 49.344 1.00 30.92 B ATOM 4624 CA SER B 744 50.955 19.277 48.245 1.00 32.47 B ATOM 4625 CB SER B 744 51.761 18.531 47.188 1.00 32.25 B ATOM 4626 OG SER B 744 51.080 17.346 46.824 1.00 29.83 B ATOM 4627 C SER B 744 49.649 19.790 47.629 1.00 34.01 B ATOM 4628 O SER B 744 49.524 21.028 47.432 1.00 35.67 B ATOM 4629 OXT SER B 744 48.778 18.934 47.348 1.00 33.32 B ATOM 4630 CB SER C 2 79.559 36.638 46.340 1.00 43.57 C ATOM 4631 OG SER C 2 79.993 37.690 45.505 1.00 44.36 C ATOM 4632 C SER C 2 78.062 35.376 44.763 1.00 44.40 C ATOM 4633 O SER C 2 78.864 34.452 44.588 1.00 45.41 C ATOM 4634 N SER C 2 77.555 35.428 47.144 1.00 45.64 C ATOM 4635 CA SER C 2 78.115 36.241 46.021 1.00 44.62 C ATOM 4636 N ASN C 3 77.108 35.678 43.890 1.00 43.20 C ATOM 4637 CA ASN C 3 76.921 34.908 42.666 1.00 41.97 C ATOM 4638 CB ASN C 3 75.435 34.551 42.505 1.00 43.04 C ATOM 4639 CG ASN C 3 74.952 33.552 43.535 1.00 43.55 C ATOM 4640 OD1 ASN C 3 75.330 32.375 43.512 1.00 43.93 C ATOM 4641 ND2 ASN C 3 74.105 34.017 44.448 1.00 43.67 C ATOM 4642 C ASN C 3 77.392 35.617 41.399 1.00 40.54 C ATOM 4643 O ASN C 3 77.723 36.800 41.401 1.00 40.39 C ATOM 4644 N VAL C 4 77.408 34.868 40.306 1.00 39.54 C ATOM 4645 CA VAL C 4 77.794 35.409 39.014 1.00 37.85 C ATOM 4646 CB VAL C 4 79.259 35.135 38.677 1.00 37.25 C ATOM 4647 CG1 VAL C 4 80.128 36.252 39.212 1.00 37.46 C ATOM 4648 CG2 VAL C 4 79.678 33.798 39.261 1.00 36.73 C ATOM 4649 C VAL C 4 76.959 34.717 37.975 1.00 36.19 C ATOM 4650 O VAL C 4 76.617 33.547 38.128 1.00 37.44 C ATOM 4651 N VAL C 5 76.627 35.440 36.917 1.00 33.92 C ATOM 4652 CA VAL C 5 75.844 34.864 35.846 1.00 31.07 C ATOM 4653 CB VAL C 5 74.812 35.871 35.315 1.00 29.79 C ATOM 4654 CG1 VAL C 5 74.186 35.342 34.041 1.00 30.11 C ATOM 4655 CG2 VAL C 5 73.735 36.100 36.359 1.00 28.61 C ATOM 4656 C VAL C 5 76.731 34.410 34.693 1.00 29.84 C ATOM 4657 O VAL C 5 77.601 35.147 34.233 1.00 29.90 C ATOM 4658 N LEU C 6 76.513 33.177 34.251 1.00 29.14 C ATOM 4659 CA LEU C 6 77.236 32.597 33.116 1.00 28.08 C ATOM 4660 CB LEU C 6 77.863 31.253 33.510 1.00 27.11 C ATOM 4661 CG LEU C 6 78.872 31.221 34.675 1.00 24.97 C ATOM 4662 CD1 LEU C 6 79.528 29.845 34.700 1.00 24.15 C ATOM 4663 CD2 LEU C 6 79.919 32.293 34.529 1.00 22.63 C ATOM 4664 C LEU C 6 76.201 32.405 31.990 1.00 27.51 C ATOM 4665 O LEU C 6 75.218 31.673 32.139 1.00 26.06 C ATOM 4666 N VAL C 7 76.422 33.083 30.869 1.00 28.04 C ATOM 4667 CA VAL C 7 75.498 33.035 29.732 1.00 29.08 C ATOM 4668 CB VAL C 7 75.410 34.425 29.046 1.00 30.10 C ATOM 4669 CG1 VAL C 7 74.517 34.349 27.805 1.00 30.31 C ATOM 4670 CG2 VAL C 7 74.887 35.454 30.033 1.00 28.75 C ATOM 4671 C VAL C 7 75.861 31.988 28.678 1.00 29.01 C ATOM 4672 O VAL C 7 77.008 31.913 28.226 1.00 28.23 C ATOM 4673 N SER C 8 74.865 31.191 28.291 1.00 28.51 C ATOM 4674 CA SER C 8 75.063 30.147 27.296 1.00 27.88 C ATOM 4675 CB SER C 8 74.009 29.037 27.418 1.00 28.20 C ATOM 4676 OG SER C 8 72.804 29.396 26.748 1.00 25.94 C ATOM 4677 C SER C 8 74.965 30.741 25.898 1.00 28.40 C ATOM 4678 O SER C 8 74.359 31.803 25.707 1.00 27.07 C ATOM 4679 N GLY C 9 75.574 30.034 24.941 1.00 27.46 C ATOM 4680 CA GLY C 9 75.569 30.450 23.553 1.00 26.64 C ATOM 4681 C GLY C 9 74.142 30.602 23.067 1.00 26.05 C ATOM 4682 O GLY C 9 73.874 31.296 22.085 1.00 26.15 C ATOM 4683 N GLU C 10 73.219 29.941 23.752 1.00 24.38 C ATOM 4684 CA GLU C 10 71.824 30.034 23.400 1.00 23.90 C ATOM 4685 CB GLU C 10 71.116 28.716 23.732 1.00 24.63 C ATOM 4686 CG GLU C 10 71.338 27.635 22.678 1.00 29.19 C ATOM 4687 CD GLU C 10 71.102 26.213 23.204 1.00 33.43 C ATOM 4688 OE1 GLU C 10 70.758 25.307 22.400 1.00 35.21 C ATOM 4689 OE2 GLU C 10 71.281 25.992 24.420 1.00 36.33 C ATOM 4690 C GLU C 10 71.186 31.221 24.133 1.00 23.12 C ATOM 4691 O GLU C 10 69.975 31.374 24.128 1.00 20.55 C ATOM 4692 N GLY C 11 72.008 32.064 24.756 1.00 25.05 C ATOM 4693 CA GLY C 11 71.491 33.228 25.458 1.00 26.75 C ATOM 4694 C GLY C 11 70.939 33.036 26.861 1.00 29.02 C ATOM 4695 O GLY C 11 70.676 34.022 27.557 1.00 28.98 C ATOM 4696 N GLU C 12 70.757 31.782 27.276 1.00 29.73 C ATOM 4697 CA GLU C 12 70.238 31.469 28.604 1.00 29.91 C ATOM 4698 CB GLU C 12 69.778 30.009 28.657 1.00 29.67 C ATOM 4699 CG GLU C 12 68.537 29.805 27.817 1.00 29.78 C ATOM 4700 CD GLU C 12 67.792 28.516 28.112 1.00 31.45 C ATOM 4701 OE1 GLU C 12 68.320 27.419 27.801 1.00 31.80 C ATOM 4702 OE2 GLU C 12 66.663 28.603 28.651 1.00 32.30 C ATOM 4703 C GLU C 12 71.231 31.769 29.730 1.00 31.37 C ATOM 4704 O GLU C 12 72.364 31.288 29.723 1.00 31.63 C ATOM 4705 N ARG C 13 70.793 32.579 30.693 1.00 32.45 C ATOM 4706 CA ARG C 13 71.642 32.983 31.807 1.00 33.31 C ATOM 4707 CB ARG C 13 71.215 34.341 32.335 1.00 33.47 C ATOM 4708 CG ARG C 13 70.328 35.124 31.392 1.00 35.00 C ATOM 4709 CD ARG C 13 69.909 36.383 32.092 1.00 35.56 C ATOM 4710 NE ARG C 13 71.082 37.195 32.375 1.00 39.21 C ATOM 4711 CZ ARG C 13 71.210 37.997 33.423 1.00 40.03 C ATOM 4712 NH1 ARG C 13 70.231 38.093 34.310 1.00 39.27 C ATOM 4713 NH2 ARG C 13 72.310 38.726 33.566 1.00 40.62 C ATOM 4714 C ARG C 13 71.607 31.997 32.949 1.00 33.28 C ATOM 4715 O ARG C 13 70.534 31.584 33.387 1.00 33.83 C ATOM 4716 N PHE C 14 72.790 31.626 33.431 1.00 33.28 C ATOM 4717 CA PHE C 14 72.916 30.692 34.545 1.00 32.01 C ATOM 4718 CB PHE C 14 73.791 29.488 34.180 1.00 32.03 C ATOM 4719 CG PHE C 14 73.173 28.552 33.175 1.00 32.79 C ATOM 4720 CD1 PHE C 14 73.005 28.935 31.850 1.00 33.70 C ATOM 4721 CD2 PHE C 14 72.815 27.256 33.545 1.00 32.47 C ATOM 4722 CE1 PHE C 14 72.491 28.032 30.910 1.00 34.61 C ATOM 4723 CE2 PHE C 14 72.301 26.349 32.620 1.00 30.80 C ATOM 4724 CZ PHE C 14 72.141 26.731 31.300 1.00 31.82 C ATOM 4725 C PHE C 14 73.560 31.394 35.733 1.00 31.30 C ATOM 4726 O PHE C 14 74.669 31.918 35.633 1.00 30.38 C ATOM 4727 N THR C 15 72.860 31.403 36.857 1.00 30.28 C ATOM 4728 CA THR C 15 73.387 32.013 38.066 1.00 29.27 C ATOM 4729 CB THR C 15 72.253 32.635 38.900 1.00 28.06 C ATOM 4730 OG1 THR C 15 71.567 33.612 38.111 1.00 27.43 C ATOM 4731 CG2 THR C 15 72.801 33.282 40.158 1.00 25.34 C ATOM 4732 C THR C 15 74.060 30.925 38.901 1.00 29.98 C ATOM 4733 O THR C 15 73.521 29.827 39.032 1.00 30.73 C ATOM 4734 N VAL C 16 75.244 31.211 39.435 1.00 30.04 C ATOM 4735 CA VAL C 16 75.943 30.254 40.291 1.00 31.88 C ATOM 4736 CB VAL C 16 76.853 29.283 39.491 1.00 32.07 C ATOM 4737 CG1 VAL C 16 76.035 28.547 38.455 1.00 35.42 C ATOM 4738 CG2 VAL C 16 77.988 30.034 38.823 1.00 34.64 C ATOM 4739 C VAL C 16 76.793 30.991 41.327 1.00 32.89 C ATOM 4740 O VAL C 16 77.097 32.176 41.168 1.00 32.60 C ATOM 4741 N ASP C 17 77.170 30.286 42.390 1.00 33.45 C ATOM 4742 CA ASP C 17 77.976 30.874 43.455 1.00 33.69 C ATOM 4743 CB ASP C 17 78.117 29.888 44.618 1.00 35.66 C ATOM 4744 CG ASP C 17 79.027 30.419 45.727 1.00 38.16 C ATOM 4745 OD1 ASP C 17 78.721 31.520 46.269 1.00 38.20 C ATOM 4746 OD2 ASP C 17 80.037 29.741 46.047 1.00 36.91 C ATOM 4747 C ASP C 17 79.347 31.221 42.911 1.00 33.45 C ATOM 4748 O ASP C 17 80.034 30.352 42.391 1.00 32.08 C ATOM 4749 N LYS C 18 79.768 32.475 43.045 1.00 35.48 C ATOM 4750 CA LYS C 18 81.068 32.853 42.495 1.00 39.15 C ATOM 4751 CB LYS C 18 81.378 34.325 42.766 1.00 40.50 C ATOM 4752 CG LYS C 18 81.886 34.630 44.144 1.00 45.70 C ATOM 4753 CD LYS C 18 82.169 36.128 44.285 1.00 48.13 C ATOM 4754 CE LYS C 18 83.245 36.589 43.318 1.00 48.38 C ATOM 4755 NZ LYS C 18 84.546 35.898 43.581 1.00 49.06 C ATOM 4756 C LYS C 18 82.212 31.978 42.993 1.00 38.99 C ATOM 4757 O LYS C 18 83.109 31.638 42.228 1.00 38.11 C ATOM 4758 N LYS C 19 82.177 31.596 44.263 1.00 39.59 C ATOM 4759 CA LYS C 19 83.232 30.759 44.813 1.00 38.98 C ATOM 4760 CB LYS C 19 82.940 30.429 46.274 0.00 39.52 C ATOM 4761 CG LYS C 19 84.077 29.703 46.968 0.00 40.25 C ATOM 4762 CD LYS C 19 83.738 29.363 48.404 0.00 40.84 C ATOM 4763 CE LYS C 19 82.586 28.380 48.468 0.00 41.18 C ATOM 4764 NZ LYS C 19 82.206 28.077 49.871 0.00 41.44 C ATOM 4765 C LYS C 19 83.364 29.470 44.010 1.00 38.49 C ATOM 4766 O LYS C 19 84.475 29.025 43.725 1.00 37.49 C ATOM 4767 N ILE C 20 82.223 28.877 43.651 1.00 39.86 C ATOM 4768 CA ILE C 20 82.167 27.631 42.858 1.00 40.16 C ATOM 4769 CB ILE C 20 80.725 27.037 42.836 1.00 39.38 C ATOM 4770 CG2 ILE C 20 80.705 25.698 42.109 1.00 38.50 C ATOM 4771 CG1 ILE C 20 80.225 26.858 44.270 1.00 39.70 C ATOM 4772 CD1 ILE C 20 78.801 26.351 44.371 1.00 41.15 C ATOM 4773 C ILE C 20 82.588 27.949 41.421 1.00 40.51 C ATOM 4774 O ILE C 20 83.424 27.272 40.841 1.00 39.84 C ATOM 4775 N ALA C 21 81.999 28.999 40.865 1.00 41.64 C ATOM 4776 CA ALA C 21 82.312 29.423 39.524 1.00 43.06 C ATOM 4777 CB ALA C 21 81.635 30.753 39.229 1.00 43.43 C ATOM 4778 C ALA C 21 83.818 29.554 39.349 1.00 43.95 C ATOM 4779 O ALA C 21 84.353 29.186 38.307 1.00 45.27 C ATOM 4780 N GLU C 22 84.506 30.090 40.354 1.00 44.60 C ATOM 4781 CA GLU C 22 85.958 30.254 40.266 1.00 44.95 C ATOM 4782 CB GLU C 22 86.546 30.773 41.582 1.00 47.05 C ATOM 4783 CG GLU C 22 86.200 32.217 41.915 1.00 50.65 C ATOM 4784 CD GLU C 22 87.063 32.769 43.035 1.00 52.85 C ATOM 4785 OE1 GLU C 22 87.098 32.164 44.125 1.00 54.88 C ATOM 4786 OE2 GLU C 22 87.716 33.809 42.826 1.00 54.85 C ATOM 4787 C GLU C 22 86.652 28.949 39.898 1.00 43.86 C ATOM 4788 O GLU C 22 87.851 28.933 39.637 1.00 43.78 C ATOM 4789 N ARG C 23 85.912 27.849 39.893 1.00 42.42 C ATOM 4790 CA ARG C 23 86.498 26.576 39.517 1.00 42.71 C ATOM 4791 CB ARG C 23 85.442 25.496 39.602 1.00 43.00 C ATOM 4792 CG ARG C 23 85.870 24.197 39.043 1.00 44.32 C ATOM 4793 CD ARG C 23 86.100 23.258 40.161 1.00 46.65 C ATOM 4794 NE ARG C 23 87.502 23.204 40.508 1.00 47.94 C ATOM 4795 CZ ARG C 23 87.967 22.532 41.548 1.00 48.45 C ATOM 4796 NE1 ARG C 23 87.122 21.875 42.338 1.00 46.40 C ATOM 4797 NH2 ARG C 23 89.274 22.493 41.768 1.00 50.58 C ATOM 4798 C ARG C 23 86.956 26.742 38.072 1.00 42.33 C ATOM 4799 O ARG C 23 87.703 25.926 37.536 1.00 41.75 C ATOM 4800 N SER C 24 86.461 27.812 37.458 1.00 42.76 C ATOM 4801 CA SER C 24 86.773 28.177 36.087 1.00 43.35 C ATOM 4802 CB SER C 24 85.531 28.757 35.406 1.00 42.29 C ATOM 4803 OC SER C 24 85.845 29.241 34.116 1.00 39.65 C ATOM 4804 C SER C 24 87.868 29.235 36.113 1.00 44.08 C ATOM 4805 O SER C 24 87.591 30.403 36.361 1.00 44.37 C ATOM 4806 N LEU C 25 89.109 28.830 35.875 1.00 45.48 C ATOM 4807 CA LEU C 25 90.217 29.773 35.875 1.00 47.35 C ATOM 4808 CB LEU C 25 91.490 29.117 35.350 1.00 48.27 C ATOM 4809 CG LEU C 25 92.107 28.027 36.219 1.00 48.77 C ATOM 4810 CD1 LEU C 25 93.392 27.506 35.595 0.00 48.78 C ATOM 4811 CD2 LEU C 25 92.365 28.610 37.598 1.00 48.53 C ATOM 4812 C LEU C 25 89.871 30.932 34.979 1.00 48.70 C ATOM 4813 O LEU C 25 90.293 32.064 35.233 1.00 48.05 C ATOM 4814 N LEU C 26 89.116 30.635 33.919 1.00 50.30 C ATOM 4815 CA LEU C 26 88.703 31.658 32.956 1.00 50.59 C ATOM 4816 CB LEU C 26 87.901 31.046 31.787 1.00 50.13 C ATOM 4817 CG LEU C 26 87.543 31.994 30.621 1.00 49.31 C ATOM 4818 CD1 LEU C 26 88.810 32.356 29.880 1.00 49.37 C ATOM 4819 CD2 LEU C 26 86.542 31.346 29.655 1.00 49.24 C ATOM 4820 C LEU C 26 87.857 32.687 33.689 1.00 50.59 C ATOM 4821 O LEU C 26 88.005 33.888 33.478 1.00 50.43 C ATOM 4822 N LEU C 27 86.980 32.210 34.562 1.00 51.20 C ATOM 4823 CA LEU C 27 86.132 33.103 35.325 1.00 53.37 C ATOM 4824 CB LEU C 27 84.930 32.324 35.871 1.00 54.39 C ATOM 4825 CG LEU C 27 83.811 33.095 36.583 1.00 55.55 C ATOM 4826 CD1 LEU C 27 84.258 33.408 37.990 1.00 56.54 C ATOM 4827 CD2 LEU C 27 83.445 34.376 35.817 1.00 55.58 C ATOM 4828 C LEU C 27 86.947 33.775 36.446 1.00 54.11 C ATOM 4829 O LEU C 27 86.669 34.918 36.822 1.00 54.13 C ATOM 4830 N LYS C 28 87.960 33.077 36.961 1.00 54.29 C ATOM 4831 CA LYS C 28 88.816 33.650 37.993 1.00 54.46 C ATOM 4832 CB LYS C 28 89.825 32.623 38.506 1.00 54.18 C ATOM 4833 CG LYS C 28 89.252 31.586 39.446 1.00 54.09 C ATOM 4834 CD LYS C 28 90.359 30.727 40.048 0.00 54.84 C ATOM 4835 CE LYS C 28 91.404 31.584 40.756 0.00 55.16 C ATOM 4836 NZ LYS C 28 90.817 32.412 41.846 0.00 55.54 C ATOM 4837 C LYS C 28 89.565 34.851 37.408 1.00 55.03 C ATOM 4838 O LYS C 28 89.502 35.943 37.956 1.00 54.89 C ATOM 4839 N ASN C 29 90.269 34.657 36.295 1.00 56.14 C ATOM 4840 CA ASN C 29 91.006 35.758 35.671 1.00 57.16 C ATOM 4841 CB ASN C 29 91.659 35.319 34.354 1.00 57.83 C ATOM 4842 CG ASN C 29 92.642 34.173 34.532 1.00 58.99 C ATOM 4843 OD1 ASN C 29 93.170 33.633 33.558 1.00 59.61 C ATOM 4844 ND2 ASN C 29 92.895 33.800 35.776 1.00 59.68 C ATOM 4845 C ASN C 29 90.071 36.923 35.375 1.00 57.45 C ATOM 4846 O ASN C 29 90.455 38.079 35.525 1.00 57.22 C ATOM 4847 N TYR C 30 88.849 36.620 34.943 1.00 57.89 C ATOM 4848 CA TYR C 30 87.882 37.664 34.615 1.00 58.66 C ATOM 4849 CB TYR C 30 86.516 37.039 34.317 1.00 57.87 C ATOM 4850 CG TYR C 30 85.636 37.872 33.409 1.00 56.71 C ATOM 4851 CD1 TYR C 30 86.054 38.229 32.133 1.00 55.67 C ATOM 4852 CE1 TYR C 30 85.231 38.968 31.282 1.00 55.50 C ATOM 4853 CD2 TYR C 30 84.373 38.276 33.818 1.00 56.61 C ATOM 4854 CE2 TYR C 30 83.539 39.014 32.979 1.00 56.59 C ATOM 4855 CZ TYR C 30 83.972 39.355 31.712 1.00 56.92 C ATOM 4856 OH TYR C 30 83.132 40.065 30.873 1.00 57.63 C ATOM 4857 C TYR C 30 87.787 38.649 35.783 1.00 60.59 C ATOM 4858 O TYR C 30 87.482 39.830 35.590 1.00 59.71 C ATOM 4859 N LEU C 31 88.062 38.146 36.989 1.00 62.33 C ATOM 4860 CA LEU C 31 88.047 38.932 38.230 1.00 62.29 C ATOM 4861 CB LEU C 31 89.371 39.712 38.370 1.00 62.08 C ATOM 4862 CG LEU C 31 89.853 40.603 37.215 1.00 61.04 C ATOM 4863 CO1 LEU C 31 89.303 42.000 37.370 1.00 60.84 C ATOM 4864 CD2 LEU C 31 91.363 40.639 37.205 1.00 61.22 C ATOM 4865 C LEU C 31 86.860 39.875 38.358 1.00 62.55 C ATOM 4866 O LEU C 31 85.754 39.555 37.917 1.00 63.88 C ATOM 4867 N ILE C 45 80.545 40.215 37.240 1.00 45.54 C ATOM 4868 CA ILE C 45 79.354 39.523 37.719 1.00 45.75 C ATOM 4869 CB ILE C 45 78.323 40.511 38.318 1.00 46.06 C ATOM 4870 CG2 ILE C 45 77.704 41.376 37.213 1.00 43.89 C ATOM 4871 CG1 ILE C 45 77.248 39.723 39.075 1.00 46.70 C ATOM 4872 CD1 ILE C 45 76.128 40.574 39.614 1.00 48.94 C ATOM 4873 C ILE C 45 78.665 38.702 36.617 1.00 45.24 C ATOM 4874 O ILE C 45 78.069 37.659 36.904 1.00 45.32 C ATOM 4875 N VAL C 46 78.758 39.158 35.364 1.00 43.40 C ATOM 4876 CA VAL C 46 78.154 38.438 34.237 1.00 41.39 C ATOM 4877 CB VAL C 46 76.974 39.226 33.613 1.00 41.64 C ATOM 4878 CG1 VAL C 46 76.308 38.378 32.531 1.00 41.02 C ATOM 4879 CG2 VAL C 46 75.962 39.604 34.690 1.00 41.38 C ATOM 4880 C VAL C 46 79.154 38.131 33.123 1.00 39.66 C ATOM 4881 O VAL C 46 79.480 39.005 32.318 1.00 40.66 C ATOM 4882 N MSE C 47 79.635 36.892 33.071 1.00 38.75 C ATOM 4883 CA MSE C 47 80.597 36.501 32.039 1.00 37.26 C ATOM 4884 CB MSE C 47 81.753 35.691 32.641 1.00 38.19 C ATOM 4885 CG MSE C 47 82.901 35.488 31.668 1.00 40.50 C ATOM 4886 SE MSE C 47 84.215 34.179 32.219 1.00 47.69 C ATOM 4887 CE MSE C 47 83.332 32.527 31.723 1.00 41.93 C ATOM 4888 C MSE C 47 79.924 35.669 30.954 1.00 34.30 C ATOM 4889 O MSE C 47 79.108 34.793 31.246 1.00 32.32 C ATOM 4890 N PRO C 48 80.240 35.954 29.682 1.00 32.53 C ATOM 4891 CD PRO C 48 80.789 37.227 29.204 1.00 31.72 C ATOM 4892 CA PRO C 48 79.655 35.207 28.566 1.00 32.32 C ATOM 4893 CB PRO C 48 79.787 36.176 27.389 1.00 31.12 C ATOM 4894 CG PRO C 48 79.872 37.514 28.049 1.00 31.73 C ATOM 4895 C PRO C 48 80.408 33.895 28.302 1.00 31.55 C ATOM 4896 O PRO C 48 81.615 33.809 28.506 1.00 32.35 C ATOM 4897 N VAL C 49 79.696 32.864 27.874 1.00 30.22 C ATOM 4898 CA VAL C 49 80.347 31.609 27.553 1.00 29.45 C ATOM 4899 CB VAL C 49 79.832 30.440 28.418 1.00 30.65 C ATOM 4900 CG1 VAL C 49 80.731 29.222 28.234 1.00 29.09 C ATOM 4901 CG2 VAL C 49 79.803 30.851 29.872 1.00 31.28 C ATOM 4902 C VAL C 49 79.958 31.389 26.105 1.00 28.38 C ATOM 4903 O VAL C 49 79.011 30.660 25.798 1.00 28.07 C ATOM 4904 N PRO C 50 80.673 32.049 25.191 1.00 27.28 C ATOM 4905 CD PRO C 50 81.736 33.036 25.433 1.00 27.20 C ATOM 4906 CA PRO C 50 80.410 31.937 23.765 1.00 26.24 C ATOM 4907 CB PRO C 50 81.504 32.810 23.158 1.00 26.55 C ATOM 4908 CG PRO C 50 81.687 33.866 24.182 1.00 25.75 C ATOM 4909 C PRO C 50 80.426 30.516 23.202 1.00 26.07 C ATOM 4910 O PRO C 50 81.292 29.698 23.529 1.00 25.12 C ATOM 4911 N ASN C 51 79.447 30.247 22.347 1.00 25.23 C ATOM 4912 CA ASN C 51 79.317 28.975 21.668 1.00 25.26 C ATOM 4913 CB ASN C 51 80.446 28.820 20.660 1.00 26.35 C ATOM 4914 CG ASN C 51 80.554 30.005 19.737 1.00 27.98 C ATOM 4915 OD1 ASN C 51 79.567 30.413 19.116 1.00 28.79 C ATOM 4916 ND2 ASN C 51 81.752 30.578 19.644 1.00 27.02 C ATOM 4917 C ASN C 51 79.299 27.762 22.558 1.00 24.62 C ATOM 4918 O ASN C 51 80.090 26.861 22.374 1.00 25.28 C ATOM 4919 N VAL C 52 78.388 27.726 23.510 1.00 25.26 C ATOM 4920 CA VAL C 52 78.284 26.592 24.395 1.00 25.46 C ATOM 4921 CB VAL C 52 78.983 26.866 25.714 1.00 27.00 C ATOM 4922 CG1 VAL C 52 78.759 25.698 26.668 1.00 26.64 C ATOM 4923 CG2 VAL C 52 80.473 27.098 25.487 1.00 27.68 C ATOM 4924 C VAL C 52 76.808 26.404 24.685 1.00 27.92 C ATOM 4925 O VAL C 52 76.181 27.275 25.305 1.00 30.25 C ATOM 4926 N ARG C 53 76.246 25.278 24.249 1.00 28.81 C ATOM 4927 CA ARG C 53 74.824 25.012 24.478 1.00 29.52 C ATOM 4928 CB ARG C 53 74.393 23.688 23.845 1.00 32.39 C ATOM 4929 CG ARG C 53 74.401 23.661 22.337 1.00 37.27 C ATOM 4930 CD ARG C 53 73.908 22.307 21.839 1.00 42.50 C ATOM 4931 NE ARG C 53 74.746 21.181 22.276 1.00 47.26 C ATOM 4932 CZ ARG C 53 74.285 20.079 22.871 1.00 49.64 C ATOM 4933 NH1 ARG C 53 72.984 19.945 23.114 1.00 48.76 C ATOM 4934 NH2 ARG C 53 75.126 19.106 23.216 1.00 50.78 C ATOM 4935 C ARG C 53 74.465 24.959 25.964 1.00 28.83 C ATOM 4936 O ARG C 53 75.226 24.471 26.794 1.00 27.65 C ATOM 4937 N SER C 54 73.274 25.454 26.268 1.00 27.01 C ATOM 4938 CA SER C 54 72.769 25.467 27.613 1.00 24.06 C ATOM 4939 CB SER C 54 71.302 25.871 27.612 1.00 22.38 C ATOM 4940 OC SER C 54 71.159 27.162 27.056 1.00 20.31 C ATOM 4941 C SER C 54 72.946 24.093 28.246 1.00 24.61 C ATOM 4942 O SER C 54 73.676 23.948 29.223 1.00 26.72 C ATOM 4943 N SER C 55 72.306 23.071 27.698 1.00 23.42 C ATOM 4944 CA SER C 55 72.455 21.735 28.268 1.00 22.33 C ATOM 4945 CB SER C 55 71.922 20.684 27.304 1.00 19.49 C ATOM 4946 OG SER C 55 72.598 20.765 26.075 1.00 22.52 C ATOM 4947 C SER C 55 73.909 21.414 28.610 1.00 21.51 C ATOM 4948 O SER C 55 74.168 20.766 29.613 1.00 23.53 C ATOM 4949 N VAL C 56 74.851 21.884 27.795 1.00 20.84 C ATOM 4950 CA VAL C 56 76.274 21.624 28.031 1.00 20.83 C ATOM 4951 CB VAL C 56 77.137 21.998 26.757 1.00 20.76 C ATOM 4952 CG1 VAL C 56 78.593 21.624 26.953 1.00 16.97 C ATOM 4953 CG2 VAL C 56 76.583 21.284 25.514 1.00 20.88 C ATOM 4954 C VAL C 56 76.768 22.418 29.260 1.00 19.61 C ATOM 4955 O VAL C 56 77.375 21.849 30.172 1.00 18.87 C ATOM 4956 N LEU C 57 76.515 23.724 29.271 1.00 19.82 C ATOM 4957 CA LEU C 57 76.906 24.588 30.379 1.00 20.45 C ATOM 4958 CB LEU C 57 76.487 26.026 30.075 1.00 17.81 C ATOM 4959 CG LEU C 57 76.896 27.099 31.084 1.00 15.76 C ATOM 4960 CD1 LEU C 57 78.375 27.066 31.281 1.00 14.13 C ATOM 4961 CD2 LEU C 57 76.451 28.463 30.589 1.00 17.83 C ATOM 4962 C LEU C 57 76.231 24.116 31.678 1.00 21.81 C ATOM 4963 O LEU C 57 76.842 24.076 32.744 1.00 22.15 C ATOM 4964 N GLN C 58 74.956 23.777 31.588 1.00 22.64 C ATOM 4965 CA GLN C 58 74.255 23.311 32.757 1.00 24.92 C ATOM 4966 CB GLN C 58 72.811 22.991 32.418 1.00 25.24 C ATOM 4967 CG GLN C 58 72.079 22.366 33.567 1.00 27.25 C ATOM 4968 CD GLN C 58 70.636 22.144 33.271 1.00 28.40 C ATOM 4969 OE1 GLN C 58 70.047 21.177 33.740 1.00 31.18 C ATOM 4970 NE2 GLN C 58 70.043 23.041 32.500 1.00 29.28 C ATOM 4971 C GLN C 58 74.938 22.065 33.282 1.00 26.17 C ATOM 4972 O GLN C 58 75.060 21.872 34.487 1.00 27.72 C ATOM 4973 N LYS C 59 75.375 21.209 32.373 1.00 27.32 C ATOM 4974 CA LYS C 59 76.047 19.990 32.771 1.00 29.09 C ATOM 4975 CB LYS C 59 76.229 19.093 31.549 1.00 29.32 C ATOM 4976 CG LYS C 59 76.548 17.651 31.869 1.00 32.80 C ATOM 4977 CD LYS C 59 75.309 16.788 31.972 1.00 32.66 C ATOM 4978 CE LYS C 59 75.708 15.346 32.280 1.00 34.41 C ATOM 4979 NZ LYS C 59 74.566 14.374 32.116 1.00 36.74 C ATOM 4980 C LYS C 59 77.406 20.346 33.412 1.00 31.23 C ATOM 4981 O LYS C 59 77.793 19.750 34.418 1.00 32.05 C ATOM 4982 N VAL C 60 78.116 21.320 32.837 1.00 31.14 C ATOM 4983 CA VAL C 60 79.416 21.769 33.350 1.00 30.44 C ATOM 4984 CB VAL C 60 80.022 22.893 32.461 1.00 30.16 C ATOM 4985 CG1 VAL C 60 81.236 23.514 33.139 1.00 28.33 C ATOM 4986 CG2 VAL C 60 80.422 22.325 31.109 1.00 32.07 C ATOM 4987 C VAL C 60 79.310 22.314 34.767 1.00 31.68 C ATOM 4988 O VAL C 60 80.078 21.953 35.650 1.00 32.71 C ATOM 4989 N ILE C 61 78.356 23.204 34.969 1.00 32.12 C ATOM 4990 CA ILE C 61 78.140 23.804 36.262 1.00 31.24 C ATOM 4991 CB ILE C 61 77.021 24.824 36.170 1.00 31.54 G ATOM 4992 CG2 ILE C 61 76.601 25.279 37.564 1.00 28.63 G ATOM 4993 CG1 ILE C 61 77.497 25.982 35.297 1.00 31.49 G ATOM 4994 CD1 ILE C 61 76.388 26.850 34.795 1.00 32.68 G ATOM 4995 C ILE C 61 77.780 22.749 37.289 1.00 31.52 G ATOM 4996 O ILE C 61 78.360 22.707 38.368 1.00 31.59 G ATOM 4997 N GLU G 62 76.836 21.881 36.955 1.00 31.93 G ATOM 4998 CA GLU G 62 76.443 20.861 37.907 1.00 33.23 G ATOM 4999 CB GLU G 62 75.295 20.025 37.375 1.00 32.43 G ATOM 5000 CG GLU G 62 75.721 18.813 36.636 1.00 34.09 G ATOM 5001 CD GLU G 62 74.649 17.762 36.649 1.00 35.90 G ATOM 5002 OE1 GLU G 62 74.307 17.292 37.757 1.00 35.78 G ATOM 5003 OE2 GLU G 62 74.143 17.408 35.558 1.00 37.89 G ATOM 5004 C GLU G 62 77.595 19.939 38.278 1.00 33.56 G ATOM 5005 O GLU G 62 77.462 19.096 39.161 1.00 34.70 G ATOM 5006 N TRP C 63 78.717 20.086 37.593 1.00 33.45 G ATOM 5007 CA TRP C 63 79.872 19.269 37.888 1.00 33.70 G ATOM 5008 CB TRP C 63 80.670 18.991 36.622 1.00 33.66 G ATOM 5009 CG TRP C 63 81.955 18.280 36.884 1.00 33.52 G ATOM 5010 CD2 TRP C 63 83.211 18.876 37.231 1.00 32.28 G ATOM 5011 CE2 TRP C 63 84.142 17.826 37.386 1.00 32.37 G ATOM 5012 CE3 TRP C 63 83.639 20.196 37.429 1.00 31.95 G ATOM 5013 CD1 TRP C 63 82.167 16.935 36.846 1.00 34.55 G ATOM 5014 NE1 TRP C 63 83.481 16.653 37.143 1.00 34.74 G ATOM 5015 CZ2 TRP C 63 85.476 18.049 37.726 1.00 32.07 G ATOM 5016 CZ3 TRP C 63 84.965 20.424 37.768 1.00 31.44 G ATOM 5017 CH2 TRP C 63 85.871 19.351 37.914 1.00 32.65 G ATOM 5018 C TRP C 63 80.726 20.067 38.853 1.00 34.67 G ATOM 5019 O TRP C 63 81.367 19.512 39.733 1.00 36.11 G ATOM 5020 N ALA C 64 80.737 21.380 38.686 1.00 36.01 C ATOM 5021 CA ALA C 64 81.537 22.234 39.551 1.00 38.09 C ATOM 5022 CB ALA C 64 81.604 23.652 38.975 1.00 38.34 C ATOM 5023 C ALA C 64 80.954 22.270 40.954 1.00 38.84 C ATOM 5024 O ALA C 64 81.653 22.010 41.928 1.00 40.17 C ATOM 5025 N GLU C 65 79.670 22.605 41.045 1.00 39.31 C ATOM 5026 CA GLU C 65 78.981 22.675 42.322 1.00 39.42 C ATOM 5027 CB GLU C 65 77.483 22.928 42.099 1.00 37.23 C ATOM 5028 CG GLU C 65 77.202 24.210 41.330 1.00 34.34 C ATOM 5029 CD GLU C 65 75.724 24.533 41.190 1.00 33.67 C ATOM 5030 OE1 GLU C 65 74.926 23.651 40.805 1.00 33.23 C ATOM 5031 OE2 GLU C 65 75.356 25.688 41.455 1.00 33.33 C ATOM 5032 C GLU C 65 79.196 21.376 43.101 1.00 41.07 C ATOM 5033 O GLU C 65 79.379 21.406 44.315 1.00 41.60 C ATOM 5034 N HIS C 66 79.190 20.240 42.403 1.00 42.63 C ATOM 5035 CA HIS C 66 79.391 18.944 43.059 1.00 44.78 C ATOM 5036 CB HIS C 66 78.988 17.796 42.119 1.00 44.20 C ATOM 5037 CG HIS C 66 79.334 16.420 42.622 1.00 44.62 C ATOM 5038 CD2 HIS C 66 78.548 15.363 42.937 1.00 43.92 C ATOM 5039 ND1 HIS C 66 80.634 15.972 42.740 1.00 45.83 C ATOM 5040 CE1 HIS C 66 80.633 14.699 43.095 1.00 43.67 C ATOM 5041 NE2 HIS C 66 79.379 14.305 43.221 1.00 42.62 C ATOM 5042 C HIS C 66 80.823 18.750 43.544 1.00 46.51 C ATOM 5043 O HIS C 66 81.063 18.025 44.505 1.00 47.99 C ATOM 5044 N HIS C 67 81.781 19.393 42.894 1.00 47.66 C ATOM 5045 CA HIS C 67 83.163 19.249 43.321 1.00 49.37 C ATOM 5046 CB HIS C 67 84.059 18.952 42.127 1.00 50.68 C ATOM 5047 CG HIS C 67 83.964 17.541 41.652 1.00 52.46 C ATOM 5048 CD2 HIS C 67 83.878 16.378 42.337 1.00 53.35 C ATOM 5049 ND1 HIS C 67 83.926 17.205 40.318 1.00 54.03 C ATOM 5050 CE1 HIS C 67 83.815 15.894 40.199 1.00 53.47 C ATOM 5051 NE2 HIS C 67 83.783 15.369 41.410 1.00 54.73 C ATOM 5052 C HIS C 67 83.634 20.496 44.013 1.00 50.00 C ATOM 5053 O HIS C 67 84.831 20.793 44.022 1.00 49.65 C ATOM 5054 N ARG C 68 82.685 21.219 44.603 1.00 50.89 C ATOM 5055 CA ARG C 68 82.996 22.468 45.295 1.00 52.52 C ATOM 5056 CB ARG C 68 81.721 23.137 45.804 1.00 51.55 C ATOM 5057 CG ARG C 68 80.882 22.281 46.708 1.00 51.00 C ATOM 5058 CD ARG C 68 79.609 23.021 47.114 1.00 51.32 C ATOM 5059 NE ARG C 68 78.436 22.163 46.984 1.00 50.65 C ATOM 5060 CZ ARG C 68 78.319 20.978 47.571 1.00 49.83 C ATOM 5061 NH1 ARG C 68 79.299 20.514 48.331 1.00 53.30 C ATOM 5062 NH2 ARG C 68 77.232 20.249 47.391 1.00 50.27 C ATOM 5063 C ARG C 68 83.967 22.310 46.442 1.00 53.96 C ATOM 5064 O ARG C 68 84.685 23.243 46.784 1.00 54.35 C ATOM 5065 N ASP C 69 83.993 21.134 47.046 1.00 56.66 C ATOM 5066 CA ASP C 69 84.905 20.921 48.150 1.00 59.49 C ATOM 5067 CB ASP C 69 84.147 20.357 49.361 1.00 58.83 C ATOM 5068 CG ASP C 69 82.957 21.232 49.774 1.00 58.82 C ATOM 5069 OD1 ASP C 69 83.161 22.430 50.067 1.00 57.19 C ATOM 5070 OD2 ASP C 69 81.814 20.718 49.806 1.00 58.80 C ATOM 5071 C ASP C 69 86.032 19.986 47.722 1.00 61.81 C ATOM 5072 O ASP C 69 87.029 19.849 48.426 1.00 64.04 C ATOM 5073 N SER C 70 85.890 19.355 46.561 1.00 62.80 C ATOM 5074 CA SER C 70 86.928 18.445 46.089 1.00 63.95 C ATOM 5075 CB SER C 70 86.501 17.796 44.777 1.00 64.08 C ATOM 5076 OG SER C 70 85.355 16.996 44.990 1.00 65.02 C ATOM 5077 C SER C 70 88.264 19.161 45.914 1.00 64.84 C ATOM 5078 O SER C 70 88.305 20.371 45.697 1.00 65.35 C ATOM 5079 N ASN C 71 89.360 18.418 46.029 1.00 65.33 C ATOM 5080 CA ASN C 71 90.678 19.015 45.878 1.00 65.77 C ATOM 5081 CB ASN C 71 91.549 18.684 47.091 1.00 67.38 C ATOM 5082 CG ASN C 71 90.805 18.874 48.409 1.00 70.03 C ATOM 5083 OD1 ASN C 71 90.234 19.943 48.673 1.00 70.29 C ATOM 5084 ND2 ASN C 71 90.807 17.832 49.246 1.00 70.86 C ATOM 5085 C ASN C 71 91.311 18.488 44.603 1.00 65.48 C ATOM 5086 O ASN C 71 91.311 17.280 44.351 1.00 65.01 C ATOM 5087 N PHE C 72 91.830 19.404 43.792 1.00 64.80 C ATOM 5088 CA PHE C 72 92.463 19.045 42.529 1.00 64.53 C ATOM 5089 CB PHE C 72 91.585 19.473 41.342 1.00 60.50 C ATOM 5090 CG PHE C 72 90.272 18.736 41.247 1.00 55.74 C ATOM 5091 CD1 PHE C 72 89.068 19.433 41.235 1.00 53.23 C ATOM 5092 CD2 PHE C 72 90.238 17.349 41.154 1.00 52.78 C ATOM 5093 CE1 PHE C 72 87.856 18.758 41.127 1.00 51.24 C ATOM 5094 CE2 PHE C 72 89.027 16.672 41.047 1.00 50.62 C ATOM 5095 CZ PHE C 72 87.837 17.378 41.034 1.00 50.12 C ATOM 5096 C PHE C 72 93.818 19.728 42.417 1.00 66.62 C ATOM 5097 O PHE C 72 93.940 20.918 42.709 1.00 67.09 C ATOM 5098 N PRO C 73 94.853 18.981 41.988 1.00 68.12 C ATOM 5099 CD PRO C 73 94.775 17.557 41.611 1.00 68.63 C ATOM 5100 CA PRO C 73 96.220 19.493 41.823 1.00 68.91 C ATOM 5101 CB PRO C 73 96.935 18.342 41.118 1.00 69.55 C ATOM 5102 CG PRO C 73 96.219 17.133 41.636 1.00 69.28 C ATOM 5103 C PRO C 73 96.257 20.778 40.990 1.00 69.17 C ATOM 5104 O PRO C 73 96.598 21.853 41.487 1.00 69.84 C ATOM 5105 N VAL C 86 90.900 7.286 36.371 1.00 88.13 C ATOM 5106 CA VAL C 86 90.597 6.804 37.711 1.00 88.42 C ATOM 5107 CB VAL C 86 91.894 6.677 38.553 1.00 87.81 C ATOM 5108 CG1 VAL C 86 92.562 5.342 38.273 0.00 87.97 C ATOM 5109 CG2 VAL C 86 92.855 7.813 38.214 1.00 86.72 C ATOM 5110 C VAL C 86 89.573 7.685 38.445 1.00 88.62 C ATOM 5111 O VAL C 86 89.901 8.362 39.423 1.00 88.93 C ATOM 5112 N ASP C 87 88.328 7.661 37.964 1.00 88.31 C ATOM 5113 CA ASP C 87 87.230 8.443 38.547 1.00 87.51 C ATOM 5114 CB ASP C 87 86.568 9.310 37.475 0.00 88.63 C ATOM 5115 CG ASP C 87 87.538 10.229 36.783 1.00 89.65 C ATOM 5116 OD1 ASP C 87 87.832 11.313 37.331 1.00 90.42 C ATOM 5117 OD2 ASP C 87 88.011 9.859 35.688 1.00 89.70 C ATOM 5118 C ASP C 87 86.150 7.559 39.166 1.00 86.41 C ATOM 5119 O ASP C 87 86.396 6.413 39.543 0.00 86.24 C ATOM 5120 N SER C 88 84.944 8.110 39.245 1.00 84.26 C ATOM 5121 CA SER C 88 83.803 7.402 39.800 1.00 82.05 C ATOM 5122 CB SER C 88 83.872 7.398 41.324 1.00 81.81 C ATOM 5123 OG SER C 88 82.634 6.987 41.874 1.00 81.31 C ATOM 5124 C SER C 88 82.508 8.067 39.360 1.00 80.69 C ATOM 5125 O SER C 88 81.919 7.704 38.342 1.00 81.28 C ATOM 5126 N TRP C 89 82.066 9.042 40.144 1.00 77.91 C ATOM 5127 CA TRP C 89 80.848 9.780 39.848 1.00 74.10 C ATOM 5128 CB TRP C 89 80.646 10.859 40.905 1.00 73.48 C ATOM 5129 CG TRP C 89 79.446 11.708 40.702 1.00 72.20 C ATOM 5130 CD2 TRP C 89 79.428 13.044 40.197 1.00 71.86 C ATOM 5131 CE2 TRP C 89 78.088 13.476 40.209 1.00 71.45 C ATOM 5132 CE3 TRP C 89 80.418 13.919 39.735 1.00 71.66 C ATOM 5133 CD1 TRP C 89 78.153 11.388 40.988 1.00 71.28 C ATOM 5134 NE1 TRP C 89 77.329 12.446 40.698 1.00 70.67 C ATOM 5135 CZ2 TRP C 89 77.711 14.750 39.780 1.00 71.55 C ATOM 5136 CZ3 TRP C 89 80.043 15.184 39.308 1.00 71.26 C ATOM 5137 CH2 TRP C 89 78.701 15.587 39.334 1.00 71.21 C ATOM 5138 C TRP C 89 80.995 10.415 38.473 1.00 72.28 C ATOM 5139 O TRP C 89 80.021 10.567 37.740 1.00 72.30 C ATOM 5140 N ASP C 90 82.229 10.779 38.136 1.00 70.00 C ATOM 5141 CA ASP C 90 82.543 11.389 36.848 1.00 67.79 C ATOM 5142 CB ASP C 90 84.011 11.810 36.808 1.00 64.52 C ATOM 5143 CG ASP C 90 84.300 13.010 37.685 1.00 61.24 C ATOM 5144 OD1 ASP C 90 83.453 13.363 38.530 1.00 59.13 C ATOM 5145 OD2 ASP C 90 85.388 13.594 37.533 1.00 58.53 C ATOM 5146 C ASP C 90 82.261 10.436 35.691 1.00 67.74 C ATOM 5147 O ASP C 90 81.888 10.868 34.597 1.00 68.39 C ATOM 5148 N ARG C 91 82.460 9.142 35.926 1.00 67.23 C ATOM 5149 CA ARG C 91 82.197 8.140 34.895 1.00 66.43 C ATOM 5150 CB ARG C 91 82.671 6.755 35.345 0.00 67.74 C ATOM 5151 CG ARG C 91 82.250 5.602 34.429 0.00 69.73 C ATOM 5152 CD ARG C 91 82.769 5.731 32.997 0.00 71.43 C ATOM 5153 NE ARG C 91 81.880 6.509 32.132 1.00 73.30 C ATOM 5154 CZ ARG C 91 81.888 6.448 30.803 1.00 73.96 C ATOM 5155 NH1 ARG C 91 82.739 5.645 30.176 1.00 75.13 C ATOM 5156 NH2 ARG C 91 81.038 7.180 30.098 1.00 73.71 C ATOM 5157 C ARG C 91 80.707 8.091 34.580 1.00 64.28 C ATOM 5158 O ARG C 91 80.322 8.005 33.416 1.00 64.65 C ATOM 5159 N GLU C 92 79.871 8.156 35.611 1.00 61.21 C ATOM 5160 CA GLU C 92 78.434 8.111 35.398 1.00 59.24 C ATOM 5161 CB GLU C 92 77.709 7.733 36.691 1.00 61.28 C ATOM 5162 CG GLU C 92 76.200 7.577 36.529 1.00 63.29 C ATOM 5163 CD GLU C 92 75.816 6.698 35.345 1.00 64.91 C ATOM 5164 OE1 GLU C 92 76.430 5.618 35.171 1.00 65.27 C ATOM 5165 OE2 GLU C 92 74.888 7.087 34.599 1.00 65.86 C ATOM 5166 C GLU C 92 77.947 9.463 34.908 1.00 56.10 C ATOM 5167 O GLU C 92 76.846 9.587 34.379 1.00 55.26 C ATOM 5168 N PHE C 93 78.786 10.473 35.088 1.00 52.97 C ATOM 5169 CA PHE C 93 78.470 11.828 34.669 1.00 49.46 C ATOM 5170 CB PHE C 93 79.271 12.821 35.504 1.00 47.72 C ATOM 5171 CG PHE C 93 79.168 14.237 35.031 1.00 46.31 C ATOM 5172 CD1 PHE C 93 77.975 14.936 35.134 1.00 46.80 C ATOM 5173 CD2 PHE C 93 80.274 14.880 34.487 1.00 46.30 C ATOM 5174 GE1 PHE C 93 77.881 16.260 34.698 1.00 46.57 C ATOM 5175 CE2 PHE C 93 80.194 16.200 34.048 1.00 45.89 C ATOM 5176 CZ PHE C 93 78.995 16.891 34.155 1.00 46.39 C ATOM 5177 C PHE C 93 78.805 12.007 33.195 1.00 48.24 C ATOM 5178 O PHE C 93 78.194 12.829 32.512 1.00 48.29 C ATOM 5179 N LEU C 94 79.777 11.241 32.706 1.00 46.95 C ATOM 5180 CA LEU C 94 80.181 11.334 31.304 1.00 46.69 C ATOM 5181 CB LEU C 94 81.711 11.421 31.201 1.00 43.72 C ATOM 5182 CG LEU C 94 82.347 12.602 31.931 1.00 42.20 C ATOM 5183 CD1 LEU C 94 83.827 12.571 31.708 1.00 42.01 C ATOM 5184 CD2 LEU C 94 81.761 13.918 31.444 1.00 40.79 C ATOM 5185 C LEU C 94 79.657 10.163 30.470 1.00 46.61 C ATOM 5186 O LEU C 94 80.084 9.950 29.331 1.00 47.53 C ATOM 5187 N LYS C 95 78.721 9.416 31.044 1.00 46.24 C ATOM 5188 CA LYS C 95 78.123 8.260 30.382 1.00 46.42 C ATOM 5189 CB LYS C 95 77.447 7.372 31.436 1.00 48.23 C ATOM 5190 CG LYS C 95 77.259 5.915 31.045 1.00 48.85 C ATOM 5191 CD LYS C 95 75.858 5.649 30.493 1.00 50.94 C ATOM 5192 CE LYS C 95 74.749 5.845 31.556 1.00 51.20 C ATOM 5193 NZ LYS C 95 74.537 7.259 32.014 1.00 49.42 C ATOM 5194 C LYS C 95 77.103 8.758 29.359 1.00 45.40 C ATOM 5195 O LYS C 95 76.000 8.222 29.234 1.00 45.79 C ATOM 5196 N VAL C 96 77.495 9.797 28.631 1.00 42.97 C ATOM 5197 CA VAL C 96 76.648 10.418 27.627 1.00 39.32 C ATOM 5198 CB VAL C 96 76.748 11.930 27.759 1.00 38.19 C ATOM 5199 CG1 VAL C 96 76.296 12.335 29.143 1.00 37.83 C ATOM 5200 CG2 VAL C 96 78.182 12.369 27.543 1.00 37.61 C ATOM 5201 C VAL C 96 77.069 9.973 26.224 1.00 39.45 C ATOM 5202 O VAL C 96 77.934 9.110 26.077 1.00 39.51 C ATOM 5203 N ASP C 97 76.448 10.545 25.197 1.00 38.96 C ATOM 5204 CA ASP C 97 76.776 10.194 23.820 1.00 38.45 C ATOM 5205 CB ASP C 97 75.596 10.485 22.907 1.00 40.12 C ATOM 5206 CG ASP C 97 75.212 11.951 22.907 1.00 41.57 C ATOM 5207 OD1 ASP C 97 76.061 12.785 23.289 1.00 41.15 C ATOM 5208 OD2 ASP C 97 74.066 12.271 22.516 1.00 42.19 C ATOM 5209 C ASP C 97 77.986 10.982 23.328 1.00 38.55 C ATOM 5210 O ASP C 97 78.331 12.014 23.893 1.00 37.77 C ATOM 5211 N GLN C 98 78.612 10.505 22.259 1.00 39.05 C ATOM 5212 CA GLN C 98 79.794 11.157 21.717 1.00 38.40 C ATOM 5213 CB GLN C 98 80.225 10.485 20.415 1.00 38.10 C ATOM 5214 CG GLN C 98 80.605 9.023 20.544 1.00 36.09 C ATOM 5215 CD GLN C 98 81.275 8.497 19.298 1.00 36.91 C ATOM 5216 OE1 GLN C 98 81.239 9.130 18.236 1.00 36.92 C ATOM 5217 NE2 GLN C 98 81.881 7.324 19.412 1.00 36.42 C ATOM 5218 C GLN C 98 79.650 12.653 21.470 1.00 39.08 C ATOM 5219 O GLN C 98 80.599 13.401 21.692 1.00 40.00 C ATOM 5220 N GLU C 99 78.486 13.088 21.001 1.00 39.22 C ATOM 5221 CA GLU C 99 78.271 14.502 20.726 1.00 40.50 C ATOM 5222 CB GLU C 99 76.891 14.717 20.126 1.00 42.47 C ATOM 5223 CG GLU C 99 76.918 15.343 18.756 1.00 45.54 C ATOM 5224 CD GLU C 99 77.806 16.577 18.697 1.00 47.73 C ATOM 5225 OE1 GLU C 99 77.552 17.541 19.462 1.00 47.01 C ATOM 5226 OE2 GLU C 99 78.757 16.577 17.881 1.00 47.67 C ATOM 5227 C GLU C 99 78.387 15.335 21.990 1.00 41.46 C ATOM 5228 O GLU C 99 78.980 16.418 21.993 1.00 41.51 C ATOM 5229 N MSE C 100 77.788 14.831 23.061 1.00 41.97 C ATOM 5230 CA MSE C 100 77.818 15.518 24.335 1.00 41.69 C ATOM 5231 CB MSE C 100 76.885 14.824 25.333 1.00 45.69 C ATOM 5232 CG MSE C 100 76.914 15.403 26.735 1.00 51.76 C ATOM 5233 SE MSE C 100 76.090 17.140 26.925 1.00 62.68 C ATOM 5234 CE MSE C 100 77.565 18.303 26.510 1.00 57.90 C ATOM 5235 C MSE C 100 79.243 15.546 24.867 1.00 39.87 C ATOM 5236 O MSE C 100 79.810 16.626 25.037 1.00 39.79 C ATOM 5237 N LEU C 101 79.835 14.376 25.115 1.00 37.39 C ATOM 5238 CA LEU C 101 81.199 14.341 25.651 1.00 34.99 C ATOM 5239 CB LEU C 101 81.809 12.938 25.539 1.00 33.34 C ATOM 5240 OG LEU C 101 83.130 12.730 26.289 1.00 30.53 C ATOM 5241 OD1 LEU C 101 82.896 12.845 27.780 1.00 31.52 C ATOM 5242 OD2 LEU C 101 83.684 11.363 25.965 1.00 30.51 C ATOM 5243 C LEU C 101 82.067 15.347 24.904 1.00 34.53 C ATOM 5244 O LEU C 101 82.753 16.184 25.516 1.00 34.23 C ATOM 5245 N TYR C 102 82.011 15.274 23.577 1.00 31.29 C ATOM 5246 CA TYR C 102 82.770 16.179 22.716 1.00 28.61 C ATOM 5247 CB TYR C 102 82.335 15.955 21.258 1.00 27.71 C ATOM 5248 CG TYR C 102 82.876 16.976 20.288 1.00 26.47 C ATOM 5249 CD1 TYR C 102 84.220 16.970 19.896 1.00 24.67 C ATOM 5250 CE1 TYR C 102 84.708 17.930 19.005 1.00 23.69 C ATOM 5251 CD2 TYR C 102 82.040 17.960 19.774 1.00 25.15 C ATOM 5252 CE2 TYR C 102 82.505 18.913 18.899 1.00 23.80 C ATOM 5253 CZ TYR C 102 83.827 18.899 18.512 1.00 23.80 C ATOM 5254 OH TYR C 102 84.237 19.853 17.626 1.00 21.51 C ATOM 5255 C TYR C 102 82.572 17.659 23.131 1.00 27.38 C ATOM 5256 O TYR C 102 83.536 18.383 23.433 1.00 23.78 C ATOM 5257 N GLU C 103 81.314 18.092 23.155 1.00 28.53 C ATOM 5258 CA GLU C 103 80.979 19.462 23.532 1.00 29.26 C ATOM 5259 CB GLU C 103 79.483 19.706 23.342 1.00 30.52 C ATOM 5260 CG GLU C 103 79.063 19.574 21.888 1.00 33.75 C ATOM 5261 CD GLU C 103 77.781 20.318 21.565 1.00 36.95 C ATOM 5262 OE1 GLU C 103 77.729 21.549 21.820 1.00 41.36 C ATOM 5263 OE2 GLU C 103 76.832 19.682 21.053 1.00 35.81 C ATOM 5264 C GLU C 103 81.397 19.817 24.954 1.00 27.19 C ATOM 5265 O GLU C 103 81.801 20.950 25.217 1.00 27.16 C ATOM 5266 N ILE C 104 81.317 18.855 25.870 1.00 26.37 C ATOM 5267 CA ILE C 104 81.717 19.114 27.254 1.00 25.70 C ATOM 5268 CB ILE C 104 81.356 17.913 28.167 1.00 25.25 C ATOM 5269 CG2 ILE C 104 82.091 17.986 29.485 1.00 25.29 C ATOM 5270 CG1 ILE C 104 79.859 17.935 28.450 1.00 25.32 C ATOM 5271 OD1 ILE C 104 79.346 16.709 29.127 1.00 25.12 C ATOM 5272 C ILE C 104 83.210 19.423 27.310 1.00 24.54 C ATOM 5273 O ILE C 104 83.614 20.452 27.848 1.00 22.76 C ATOM 5274 N ILE C 105 84.011 18.528 26.731 1.00 24.67 C ATOM 5275 CA ILE C 105 85.464 18.687 26.673 1.00 23.37 C ATOM 5276 CB ILE C 105 86.120 17.563 25.834 1.00 22.40 C ATOM 5277 CG2 ILE C 105 87.524 17.985 25.410 1.00 22.41 C ATOM 5278 CG1 ILE C 105 86.143 16.249 26.630 1.00 22.74 C ATOM 5279 CD1 ILE C 105 86.616 15.035 25.826 1.00 19.84 C ATOM 5280 C ILE C 105 85.844 20.038 26.057 1.00 24.11 C ATOM 5281 O ILE C 105 86.885 20.601 26.383 1.00 23.21 C ATOM 5282 N LEU C 106 85.007 20.568 25.170 1.00 25.59 C ATOM 5283 CA LEU C 106 85.341 21.845 24.546 1.00 26.22 C ATOM 5284 CB LEU C 106 84.550 22.060 23.251 1.00 24.35 C ATOM 5285 CG LEU C 106 84.955 21.288 21.982 1.00 24.05 C ATOM 5286 CD1 LEU C 106 84.041 21.702 20.824 1.00 19.50 C ATOM 5287 CD2 LEU C 106 86.411 21.582 21.631 1.00 19.81 C ATOM 5288 C LEU C 106 85.051 22.972 25.504 1.00 27.00 C ATOM 5289 O LEU C 106 85.876 23.871 25.700 1.00 28.04 C ATOM 5290 N ALA C 107 83.870 22.908 26.107 1.00 27.32 C ATOM 5291 CA ALA C 107 83.432 23.921 27.054 1.00 27.07 C ATOM 5292 CB ALA C 107 82.044 23.574 27.562 1.00 27.09 C ATOM 5293 C ALA C 107 84.417 23.967 28.210 1.00 26.97 C ATOM 5294 O ALA C 107 84.759 25.040 28.720 1.00 25.71 C ATOM 5295 N ALA C 108 84.866 22.786 28.621 1.00 27.46 C ATOM 5296 CA ALA C 108 85.809 22.688 29.726 1.00 28.55 C ATOM 5297 CB ALA C 108 86.059 21.230 30.069 1.00 27.60 C ATOM 5298 C ALA C 108 87.119 23.383 29.363 1.00 29.01 C ATOM 5299 O ALA C 108 87.595 24.264 30.085 1.00 29.74 C ATOM 5300 N ASN C 109 87.684 22.988 28.227 1.00 28.31 C ATOM 5301 CA ASN C 109 88.934 23.554 27.723 1.00 27.27 C ATOM 5302 CB ASN C 109 89.213 22.988 26.323 1.00 27.05 C ATOM 5303 CG ASN C 109 90.436 23.594 25.666 1.00 24.65 C ATOM 5304 OD1 ASN C 109 91.542 23.472 26.167 1.00 22.66 C ATOM 5305 ND2 ASN C 109 90.236 24.235 24.517 1.00 24.60 C ATOM 5306 C ASN C 109 88.848 25.074 27.661 1.00 27.03 C ATOM 5307 O ASN C 109 89.755 25.770 28.109 1.00 28.21 C ATOM 5308 N TYR C 110 87.743 25.575 27.118 1.00 26.52 C ATOM 5309 CA TYR C 110 87.528 27.003 26.969 1.00 26.57 C ATOM 5310 CE TYR C 110 86.268 27.267 26.139 1.00 25.48 C ATOM 5311 CG TYR C 110 85.938 28.734 26.018 1.00 24.82 C ATOM 5312 CD1 TYR C 110 86.780 29.596 25.317 1.00 26.81 C ATOM 5313 CE1 TYR C 110 86.543 30.968 25.273 1.00 26.16 C ATOM 5314 CD2 TYR C 110 84.838 29.282 26.669 1.00 24.41 C ATOM 5315 CE2 TYR C 110 84.596 30.658 26.628 1.00 24.83 C ATOM 5316 CZ TYR C 110 85.455 31.486 25.930 1.00 24.87 C ATOM 5317 OH TYR C 110 85.234 32.835 25.889 1.00 25.53 C ATOM 5318 C TYR C 110 87.371 27.682 28.308 1.00 27.74 C ATOM 5319 O TYR C 110 87.907 28.767 28.546 1.00 27.37 C ATOM 5320 N LEU C 111 86.610 27.040 29.178 1.00 28.23 C ATOM 5321 CA LEU C 111 86.348 27.593 30.485 1.00 28.18 C ATOM 5322 CE LEU C 111 85.067 26.958 31.031 1.00 25.97 C ATOM 5323 CG LEU C 111 83.874 27.827 31.434 1.00 24.04 C ATOM 5324 CD1 LEU C 111 83.755 29.132 30.657 1.00 19.70 C ATOM 5325 CD2 LEU C 111 82.653 26.963 31.273 1.00 24.33 C ATOM 5326 C LEU C 111 87.547 27.373 31.410 1.00 29.42 C ATOM 5327 O LEU C 111 87.524 27.765 32.578 1.00 31.45 C ATOM 5328 N ASN C 112 88.601 26.761 30.875 1.00 29.81 C ATOM 5329 CA ASN C 112 89.825 26.513 31.640 1.00 31.10 C ATOM 5330 CB ASN C 112 90.498 27.835 32.006 1.00 31.09 C ATOM 5331 CG ASN C 112 91.974 27.673 32.371 1.00 32.09 C ATOM 5332 OD1 ASN C 112 92.448 26.579 32.719 1.00 29.20 C ATOM 5333 ND2 ASN C 112 92.708 28.783 32.300 1.00 33.07 C ATOM 5334 C ASN C 112 89.563 25.740 32.927 1.00 32.17 C ATOM 5335 O ASN C 112 89.805 26.237 34.030 1.00 33.29 C ATOM 5336 N ILE C 113 89.055 24.527 32.789 1.00 31.11 C ATOM 5337 CA ILE C 113 88.798 23.717 33.954 1.00 30.18 C ATOM 5338 CE ILE C 113 87.322 23.467 34.163 1.00 30.05 C ATOM 5339 CG2 ILE C 113 87.131 22.660 35.442 1.00 28.92 C ATOM 5340 CG1 ILE C 113 86.564 24.789 34.234 1.00 28.96 C ATOM 5341 CD1 ILE C 113 85.076 24.575 34.283 1.00 28.52 C ATOM 5342 C ILE C 113 89.473 22.384 33.751 1.00 30.85 C ATOM 5343 O ILE C 113 88.834 21.400 33.387 1.00 29.72 C ATOM 5344 N LYS C 114 90.778 22.368 33.998 1.00 31.38 C ATOM 5345 CA LYS C 114 91.595 21.173 33.838 1.00 31.36 C ATOM 5346 CB LYS C 114 93.003 21.440 34.383 1.00 32.37 C ATOM 5347 CG LYS C 114 93.901 20.219 34.344 1.00 34.25 C ATOM 5348 CD LYS C 114 95.372 20.555 34.550 1.00 35.39 C ATOM 5349 CE LYS C 114 96.190 19.289 34.455 1.00 36.88 C ATOM 5350 NZ LYS C 114 95.863 18.587 33.190 1.00 40.06 C ATOM 5351 C LYS C 114 91.035 19.876 34.437 1.00 30.61 C ATOM 5352 O LYS C 114 91.054 18.841 33.785 1.00 30.70 C ATOM 5353 N PRO C 115 90.530 19.916 35.681 1.00 30.70 C ATOM 5354 CD PRO C 115 90.401 21.106 36.545 1.00 31.09 C ATOM 5355 CA PRO C 115 89.970 18.719 36.338 1.00 30.04 C ATOM 5356 CB PRO C 115 89.365 19.276 37.626 1.00 30.45 C ATOM 5357 CG PRO C 115 90.220 20.489 37.912 1.00 31.85 C ATOM 5358 C PRO C 115 88.914 18.030 35.482 1.00 29.80 C ATOM 5359 O PRO C 115 88.935 16.806 35.295 1.00 30.05 C ATOM 5360 N LEU C 116 87.981 18.833 34.974 1.00 29.91 C ATOM 5361 CA LEU C 116 86.904 18.330 34.114 1.00 29.38 C ATOM 5362 CB LEU C 116 85.797 19.376 33.980 1.00 27.77 C ATOM 5363 CG LEU C 116 84.628 18.909 33.138 1.00 27.38 C ATOM 5364 CD1 LEU C 116 84.043 17.676 33.768 1.00 27.48 C ATOM 5365 CD2 LEU C 116 83.597 20.023 33.027 1.00 27.97 C ATOM 5366 C LEU C 116 87.464 17.974 32.731 1.00 28.24 C ATOM 5367 O LEU C 116 87.042 17.003 32.107 1.00 28.34 C ATOM 5368 N LEU C 117 88.433 18.756 32.272 1.00 26.39 C ATOM 5369 CA LEU C 117 89.051 18.494 30.993 1.00 26.69 C ATOM 5370 CB LEU C 117 90.112 19.547 30.701 1.00 24.99 C ATOM 5371 CG LEU C 117 90.893 19.362 29.397 1.00 24.42 C ATOM 5372 CD1 LEU C 117 89.943 19.112 28.225 1.00 23.60 C ATOM 5373 CD2 LEU C 117 91.738 20.593 29.154 1.00 22.70 C ATOM 5374 C LEU C 117 89.680 17.100 30.981 1.00 28.34 C ATOM 5375 O LEU C 117 89.397 16.288 30.093 1.00 29.22 C ATOM 5376 N ASP C 118 90.528 16.826 31.973 1.00 29.30 C ATOM 5377 CA ASP C 118 91.207 15.532 32.105 1.00 29.52 C ATOM 5378 CB ASP C 118 92.117 15.538 33.347 1.00 32.96 C ATOM 5379 CG ASP C 118 93.158 16.668 33.316 1.00 36.46 C ATOM 5380 OD1 ASP C 118 93.138 17.470 32.353 1.00 37.36 C ATOM 5381 OD2 ASP C 118 93.990 16.757 34.253 1.00 36.80 C ATOM 5382 C ASP C 118 90.213 14.365 32.186 1.00 28.84 C ATOM 5383 O ASP C 118 90.289 13.418 31.391 1.00 28.39 C ATOM 5384 N ALA C 119 89.288 14.419 33.142 1.00 26.34 C ATOM 5385 CA ALA C 119 88.293 13.348 33.262 1.00 25.58 C ATOM 5386 CB ALA C 119 87.208 13.741 34.258 1.00 26.08 C ATOM 5387 C ALA C 119 87.654 13.022 31.899 1.00 24.81 C ATOM 5388 O ALA C 119 87.489 11.852 31.540 1.00 23.57 C ATOM 5389 N GLY C 120 87.282 14.060 31.154 1.00 22.99 C ATOM 5390 CA GLY C 120 86.695 13.840 29.850 1.00 23.36 C ATOM 5391 C GLY C 120 87.654 13.095 28.932 1.00 23.32 C ATOM 5392 O GLY C 120 87.284 12.124 28.282 1.00 22.39 C ATOM 5393 N CYS C 121 88.902 13.541 28.901 1.00 23.17 C ATOM 5394 CA CYS C 121 89.918 12.935 28.065 1.00 23.66 C ATOM 5395 CB CYS C 121 91.184 13.762 28.144 1.00 24.22 C ATOM 5396 SG CYS C 121 90.981 15.370 27.390 1.00 31.59 C ATOM 5397 C CYS C 121 90.215 11.497 28.425 1.00 24.08 C ATOM 5398 O CYS C 121 90.601 10.703 27.570 1.00 25.40 C ATOM 5399 N LYS C 122 90.026 11.155 29.692 1.00 25.04 C ATOM 5400 CA LYS C 122 90.270 9.796 30.138 1.00 24.59 C ATOM 5401 CB LYS C 122 90.293 9.740 31.672 1.00 25.68 C ATOM 5402 CG LYS C 122 91.396 10.599 32.270 1.00 26.14 C ATOM 5403 CD LYS C 122 91.580 10.400 33.763 1.00 27.91 C ATOM 5404 CE LYS C 122 92.594 11.421 34.315 1.00 29.43 C ATOM 5405 NZ LYS C 122 93.121 11.095 35.679 1.00 31.16 C ATOM 5406 C LYS C 122 89.179 8.897 29.571 1.00 24.85 C ATOM 5407 O LYS C 122 89.451 7.798 29.080 1.00 24.38 C ATOM 5408 N VAL C 123 87.940 9.366 29.611 1.00 26.05 C ATOM 5409 CA VAL C 123 86.856 8.555 29.071 1.00 27.70 C ATOM 5410 CE VAL C 123 85.509 9.274 29.197 1.00 28.31 C ATOM 5411 CG1 VAL C 123 84.389 8.383 28.667 1.00 28.23 C ATOM 5412 CG2 VAL C 123 85.272 9.627 30.650 1.00 26.87 C ATOM 5413 C VAL C 123 87.142 8.223 27.606 1.00 27.72 C ATOM 5414 O VAL C 123 86.946 7.083 27.165 1.00 27.83 C ATOM 5415 N VAL C 124 87.618 9.212 26.855 1.00 27.26 C ATOM 5416 CA VAL C 124 87.947 8.982 25.452 1.00 27.88 C ATOM 5417 CB VAL C 124 88.458 10.274 24.776 1.00 26.84 C ATOM 5418 CG1 VAL C 124 88.953 9.959 23.368 1.00 26.47 C ATOM 5419 CG2 VAL C 124 87.322 11.304 24.713 1.00 23.58 C ATOM 5420 C VAL C 124 89.008 7.880 25.343 1.00 28.21 C ATOM 5421 O VAL C 124 88.830 6.898 24.599 1.00 27.09 C ATOM 5422 N ALA C 125 90.097 8.041 26.095 1.00 26.95 C ATOM 5423 CA ALA C 125 91.170 7.050 26.102 1.00 29.33 C ATOM 5424 CB ALA C 125 92.268 7.479 27.044 1.00 27.76 C ATOM 5425 C ALA C 125 90.653 5.661 26.501 1.00 31.95 C ATOM 5426 O ALA C 125 91.063 4.647 25.930 1.00 32.25 C ATOM 5427 N GLU C 126 89.749 5.617 27.476 1.00 34.71 C ATOM 5428 CA CLU C 126 89.179 4.356 27.919 1.00 36.70 C ATOM 5429 CE GLU C 126 88.333 4.572 29.173 1.00 39.48 C ATOM 5430 CG GLU C 126 87.803 3.290 29.782 1.00 45.29 C ATOM 5431 CD GLU C 126 88.919 2.320 30.166 1.00 50.81 C ATOM 5432 OE1 GLU C 126 89.934 2.813 30.740 1.00 52.04 C ATOM 5433 OE2 GLU C 126 88.780 1.083 29.904 1.00 50.45 C ATOM 5434 C GLU C 126 88.325 3.739 26.813 1.00 35.98 C ATOM 5435 O GLU C 126 87.849 2.628 26.968 1.00 33.64 C ATOM 5436 N MSE C 127 88.123 4.477 25.717 1.00 37.74 C ATOM 5437 CA MSE C 127 87.355 3.994 24.563 1.00 39.73 C ATOM 5438 CB MSE C 127 86.592 5.129 23.866 1.00 41.63 C ATOM 5439 CG MSE C 127 85.526 5.848 24.700 1.00 42.19 C ATOM 5440 SE MSE C 127 84.412 7.110 23.629 1.00 43.57 C ATOM 5441 CE MSE C 127 82.969 5.916 23.133 1.00 43.96 C ATOM 5442 C MSE C 127 88.295 3.377 23.530 1.00 40.34 C ATOM 5443 O MSE C 127 87.885 2.517 22.753 1.00 41.30 C ATOM 5444 N ILE C 128 89.544 3.835 23.506 1.00 40.42 C ATOM 5445 CA ILE C 128 90.516 3.309 22.559 1.00 39.85 C ATOM 5446 CE ILE C 128 91.552 4.378 22.130 1.00 39.70 C ATOM 5447 CG2 ILE C 128 92.689 3.746 21.349 1.00 39.51 C ATOM 5448 CG1 ILE C 128 90.879 5.426 21.254 1.00 38.45 C ATOM 5449 CD1 ILE C 128 90.118 6.401 22.035 1.00 40.80 C ATOM 5450 C ILE C 128 91.245 2.174 23.224 1.00 39.58 C ATOM 5451 O ILE C 128 91.534 1.156 22.603 1.00 40.22 C ATOM 5452 N ARG C 129 91.518 2.353 24.508 1.00 39.78 C ATOM 5453 CA ARG C 129 92.230 1.362 25.300 1.00 38.47 C ATOM 5454 CB ARG C 129 91.959 1.599 26.781 1.00 39.40 C ATOM 5455 CG ARG C 129 93.052 1.083 27.689 1.00 38.81 C ATOM 5456 CD ARG C 129 92.731 1.379 29.130 1.00 40.09 C ATOM 5457 NE ARG C 129 92.640 2.812 29.456 1.00 42.40 C ATOM 5458 CZ ARG C 129 93.651 3.680 29.437 1.00 41.54 C ATOM 5459 NH1 ARG C 129 94.869 3.283 29.089 1.00 41.83 C ATOM 5460 NH2 ARG C 129 93.443 4.937 29.815 1.00 39.32 C ATOM 5461 C ARG C 129 91.863 −0.066 24.940 1.00 37.14 C ATOM 5462 O ARG C 129 90.682 −0.428 24.875 1.00 34.49 C ATOM 5463 N CLY C 130 92.900 −0.860 24.688 1.00 36.58 C ATOM 5464 CA GLY C 130 92.732 −2.264 24.356 1.00 36.84 C ATOM 5465 C GLY C 130 92.098 −2.656 23.032 1.00 36.85 C ATOM 5466 O GLY C 130 92.210 −3.816 22.626 1.00 37.50 C ATOM 5467 N ARG C 131 91.431 −1.721 22.359 1.00 37.11 C ATOM 5468 CA ARG C 131 90.787 −2.017 21.073 1.00 37.10 C ATOM 5469 CB ARG C 131 89.711 −0.973 20.771 1.00 39.22 C ATOM 5470 CG ARG C 131 88.431 −1.131 21.569 1.00 41.84 C ATOM 5471 CD ARG C 131 87.839 −2.509 21.363 1.00 45.09 C ATOM 5472 NE ARG C 131 86.396 −2.558 21.604 1.00 47.90 C ATOM 5473 CZ ARG C 131 85.479 −2.055 20.780 1.00 49.21 C ATOM 5474 NH1 ARG C 131 85.846 −1.459 19.656 1.00 49.53 C ATOM 5475 NH2 ARG C 131 84.191 −2.155 21.073 1.00 51.64 C ATOM 5476 C ARG C 131 91.760 −2.084 19.894 1.00 35.38 C ATOM 5477 O ARG C 131 92.917 −1.676 19.989 1.00 34.16 C ATOM 5478 N SER C 132 91.277 −2.610 18.781 1.00 33.40 C ATOM 5479 CA SER C 132 92.093 −2.717 17.585 1.00 32.90 C ATOM 5480 CB SER C 132 91.933 −4.096 16.966 1.00 31.03 C ATOM 5481 OC SER C 132 90.581 −4.307 16.607 1.00 31.69 C ATOM 5482 C SER C 132 91.646 −1.661 16.576 1.00 32.11 C ATOM 5483 O SER C 132 90.585 −1.054 16.738 1.00 30.91 C ATOM 5484 N PRO C 133 92.462 −1.422 15.532 1.00 31.16 C ATOM 5485 CD PRO C 133 93.848 −1.900 15.407 1.00 29.35 C ATOM 5486 CA PRO C 133 92.180 −0.451 14.480 1.00 32.65 C ATOM 5487 CB PRO C 133 93.219 −0.801 13.441 1.00 29.52 C ATOM 5488 CG PRO C 133 94.400 −1.021 14.307 1.00 29.23 C ATOM 5489 C PRO C 133 90.754 −0.514 13.963 1.00 35.83 C ATOM 5490 O PRO C 133 90.054 0.504 13.909 1.00 36.35 C ATOM 5491 N GLU C 134 90.318 −1.709 13.588 1.00 38.45 C ATOM 5492 CA GLU C 134 88.962 −1.875 13.104 1.00 41.11 C ATOM 5493 CB GLU C 134 88.765 −3.265 12.494 1.00 44.05 C ATOM 5494 CG GLU C 134 88.697 −3.264 10.965 1.00 49.94 C ATOM 5495 CD GLU C 134 87.779 −2.177 10.405 1.00 52.39 C ATOM 5496 OE1 GLU C 134 86.664 −2.011 10.958 1.00 54.43 C ATOM 5497 OE2 GLU C 134 88.173 −1.503 9.413 1.00 51.18 C ATOM 5498 C GLU C 134 87.968 −1.660 14.249 1.00 41.19 C ATOM 5499 O GLU C 134 86.913 −1.040 14.062 1.00 40.64 C ATOM 5500 N GLU C 135 88.297 −2.162 15.437 1.00 41.33 C ATOM 5501 CA GLU C 135 87.399 −1.978 16.575 1.00 42.01 C ATOM 5502 CB GLU C 135 87.915 −2.697 17.820 1.00 42.98 C ATOM 5503 CG GLU C 135 87.961 −4.198 17.745 1.00 44.16 C ATOM 5504 CD GLU C 135 88.393 −4.796 19.073 1.00 46.95 C ATOM 5505 OE1 GLU C 135 89.419 −4.323 19.629 1.00 46.77 C ATOM 5506 OE2 GLU C 135 87.712 −5.728 19.565 1.00 48.28 C ATOM 5507 C GLU C 135 87.226 −0.489 16.908 1.00 40.82 C ATOM 5508 O GLU C 135 86.152 −0.055 17.328 1.00 42.69 C ATOM 5509 N ILE C 136 88.284 0.292 16.718 1.00 37.69 C ATOM 5510 CA ILE C 136 88.224 1.718 16.997 1.00 33.59 C ATOM 5511 CB ILE C 136 89.638 2.316 17.096 1.00 32.05 C ATOM 5512 CG2 ILE C 136 89.552 3.838 17.349 1.00 27.02 C ATOM 5513 CG1 ILE C 136 90.412 1.564 18.196 1.00 29.01 C ATOM 5514 CD1 ILE C 136 91.859 1.992 18.390 1.00 26.23 C ATOM 5515 C ILE C 136 87.442 2.419 15.903 1.00 33.18 C ATOM 5516 O ILE C 136 86.631 3.299 16.171 1.00 31.83 C ATOM 5517 N ARG C 137 87.669 2.021 14.661 1.00 34.42 C ATOM 5518 CA ARG C 137 86.955 2.652 13.566 1.00 34.64 C ATOM 5519 CB ARG C 137 87.352 2.008 12.253 1.00 33.73 C ATOM 5520 CG ARG C 137 88.809 2.218 11.916 1.00 34.55 C ATOM 5521 CD ARG C 137 89.226 1.238 10.851 1.00 34.62 C ATOM 5522 NE ARG C 137 90.665 1.216 10.644 1.00 33.99 C ATOM 5523 CZ ARG C 137 91.340 0.120 10.328 1.00 34.12 C ATOM 5524 NH1 ARG C 137 90.694 −1.029 10.197 1.00 32.84 C ATOM 5525 NH2 ARG C 137 92.651 0.176 10.125 1.00 34.77 C ATOM 5526 C ARG C 137 85.454 2.549 13.774 1.00 35.03 C ATOM 5527 O ARG C 137 84.745 3.538 13.638 1.00 34.65 C ATOM 5528 N ARG C 138 84.968 1.366 14.132 1.00 35.13 C ATOM 5529 CA ARG C 138 83.539 1.211 14.328 1.00 36.00 C ATOM 5530 CB ARG C 138 83.176 −0.270 14.439 1.00 38.78 C ATOM 5531 CG ARG C 138 83.339 −1.037 13.114 1.00 43.46 C ATOM 5532 CD ARG C 138 82.329 −0.608 12.030 0.00 47.14 C ATOM 5533 NE ARG C 138 82.537 0.734 11.466 0.00 51.00 C ATOM 5534 CZ ARG C 138 83.462 1.061 10.563 1.00 54.05 C ATOM 5535 NH1 ARG C 138 84.302 0.146 10.095 1.00 55.91 C ATOM 5536 NH2 ARG C 138 83.532 2.307 10.105 1.00 54.20 C ATOM 5537 C ARG C 138 83.008 1.990 15.528 1.00 34.39 C ATOM 5538 O ARG C 138 81.816 2.264 15.626 1.00 34.40 C ATOM 5539 N THR C 139 83.895 2.377 16.426 1.00 31.97 C ATOM 5540 CA THR C 139 83.486 3.123 17.596 1.00 29.98 C ATOM 5541 CB THR C 139 84.575 3.077 18.624 1.00 30.24 C ATOM 5542 OG1 THR C 139 84.946 1.713 18.825 1.00 31.86 C ATOM 5543 CG2 THR C 139 84.120 3.697 19.923 1.00 28.26 C ATOM 5544 C THR C 139 83.214 4.573 17.265 1.00 29.86 C ATOM 5545 O THR C 139 82.267 5.180 17.767 1.00 30.37 C ATOM 5546 N PHE C 140 84.053 5.138 16.415 1.00 29.19 C ATOM 5547 CA PHE C 140 83.883 6.525 16.045 1.00 28.27 C ATOM 5548 CB PHE C 140 85.229 7.230 16.152 1.00 25.82 C ATOM 5549 CG PHE C 140 85.797 7.223 17.537 1.00 23.52 C ATOM 5550 CD1 PHE C 140 85.228 7.990 18.543 1.00 22.27 C ATOM 5551 CD2 PHE C 140 86.907 6.452 17.844 1.00 22.34 C ATOM 5552 CE1 PHE C 140 85.767 7.982 19.839 1.00 20.23 C ATOM 5553 CE2 PHE C 140 87.450 6.441 19.135 1.00 18.70 C ATOM 5554 CZ PHE C 140 86.880 7.204 20.126 1.00 17.04 C ATOM 5555 C PHE C 140 83.307 6.697 14.647 1.00 28.75 C ATOM 5556 O PHE C 140 83.087 7.822 14.221 1.00 30.09 C ATOM 5557 N ASN C 141 83.027 5.585 13.964 1.00 29.40 C ATOM 5558 CA ASN C 141 82.521 5.589 12.580 1.00 30.10 C ATOM 5559 CB ASN C 141 81.182 6.335 12.434 1.00 30.86 C ATOM 5560 CG ASN C 141 80.620 6.279 10.991 1.00 32.35 C ATOM 5561 OD1 ASN C 141 80.549 5.206 10.385 1.00 30.84 C ATOM 5562 ND2 ASN C 141 80.212 7.436 10.453 1.00 32.26 C ATOM 5563 C ASN C 141 83.554 6.256 11.680 1.00 30.32 C ATOM 5564 O ASN C 141 83.223 7.047 10.803 1.00 31.59 C ATOM 5565 N ILE C 142 84.821 5.953 11.907 1.00 29.73 C ATOM 5566 CA ILE C 142 85.867 6.548 11.091 1.00 30.11 C ATOM 5567 CB ILE C 142 87.151 6.830 11.983 1.00 29.75 C ATOM 5568 CG2 ILE C 142 87.180 5.925 13.180 1.00 31.60 C ATOM 5569 CG1 ILE C 142 88.428 6.712 11.164 1.00 29.84 C ATOM 5570 CD1 ILE C 142 88.925 8.056 10.663 1.00 36.02 C ATOM 5571 C ILE C 142 86.129 5.630 9.885 1.00 28.78 C ATOM 5572 O ILE C 142 86.070 4.412 10.004 1.00 27.70 C ATOM 5573 N VAL C 143 86.355 6.201 8.708 1.00 28.81 C ATOM 5574 CA VAL C 143 86.594 5.344 7.556 1.00 28.92 C ATOM 5575 CB VAL C 143 86.022 5.937 6.250 1.00 27.33 C ATOM 5576 CG1 VAL C 143 86.549 5.165 5.056 1.00 27.92 C ATOM 5577 CG2 VAL C 143 84.494 5.866 6.269 1.00 26.26 C ATOM 5578 C VAL C 143 88.071 5.084 7.356 1.00 28.95 C ATOM 5579 O VAL C 143 88.905 5.971 7.539 1.00 31.52 C ATOM 5580 N ASN C 144 88.387 3.845 7.006 1.00 27.50 C ATOM 5581 CA ASN C 144 89.754 3.434 6.761 1.00 26.06 C ATOM 5582 CB ASN C 144 89.837 1.907 6.798 1.00 27.42 C ATOM 5583 CG ASN C 144 91.258 1.377 6.661 1.00 28.39 C ATOM 5584 OD1 ASN C 144 91.528 0.242 7.035 1.00 28.70 C ATOM 5585 ND2 ASN C 144 92.162 2.185 6.119 1.00 30.75 C ATOM 5586 C ASN C 144 90.074 3.942 5.371 1.00 26.48 C ATOM 5587 O ASN C 144 89.519 3.458 4.394 1.00 26.51 C ATOM 5588 N ASP C 145 90.964 4.918 5.277 1.00 26.34 C ATOM 5589 CA ASP C 145 91.315 5.492 3.988 1.00 27.61 C ATOM 5590 CB ASP C 145 91.245 7.018 4.058 1.00 28.15 C ATOM 5591 CG ASP C 145 91.840 7.570 5.336 1.00 28.20 C ATOM 5592 OD1 ASP C 145 92.508 6.808 6.080 1.00 26.63 C ATOM 5593 OD2 ASP C 145 91.639 8.780 5.595 1.00 29.52 C ATOM 5594 C ASP C 145 92.684 5.086 3.479 1.00 28.92 C ATOM 5595 O ASP C 145 93.208 5.708 2.549 1.00 29.06 C ATOM 5596 N PHE C 146 93.262 4.050 4.083 1.00 28.68 C ATOM 5597 CA PHE C 146 94.585 3.572 3.685 1.00 29.48 C ATOM 5598 CB PHE C 146 95.222 2.744 4.799 1.00 31.05 C ATOM 5599 CG PHE C 146 95.709 3.550 5.955 1.00 33.63 C ATOM 5600 CO1 PHE C 146 96.641 4.574 5.761 1.00 34.53 C ATOM 5601 CD2 PHE C 146 95.277 3.254 7.250 1.00 33.58 C ATOM 5602 CE1 PHE C 146 97.147 5.292 6.841 1.00 35.14 C ATOM 5603 CE2 PHE C 146 95.767 3.956 8.338 1.00 34.74 C ATOM 5604 CZ PHE C 146 96.709 4.981 8.136 1.00 36.19 C ATOM 5605 C PHE C 146 94.596 2.727 2.431 1.00 28.86 C ATOM 5606 O PHE C 146 93.889 1.725 2.355 1.00 30.57 C ATOM 5607 N THR C 147 95.423 3.109 1.460 1.00 28.83 C ATOM 5608 CA THR C 147 95.536 2.339 0.222 1.00 30.01 C ATOM 5609 CB THR C 147 96.556 2.946 −0.783 1.00 29.36 C ATOM 5610 OG1 THR C 147 97.817 3.147 −0.128 1.00 29.97 C ATOM 5611 CG2 THR C 147 96.046 4.252 −1.355 1.00 27.00 C ATOM 5612 C THR C 147 96.049 0.948 0.552 1.00 30.37 C ATOM 5613 O THR C 147 96.708 0.745 1.563 1.00 31.13 C ATOM 5614 N PRO C 148 95.751 −0.032 −0.299 1.00 31.61 C ATOM 5615 CD PRO C 148 94.879 −0.031 −1.485 1.00 31.67 C ATOM 5616 CA PRO C 148 96.241 −1.375 −0.010 1.00 32.60 C ATOM 5617 CB PRO C 148 95.903 −2.141 −1.282 1.00 31.26 C ATOM 5618 CG PRO C 148 94.611 −1.527 −1.697 1.00 30.19 C ATOM 5619 C PRO C 148 97.734 −1.327 0.255 1.00 34.28 C ATOM 5620 O PRO C 148 98.244 −2.067 1.087 1.00 35.43 C ATOM 5621 N GLU C 149 98.441 −0.445 −0.437 1.00 37.73 C ATOM 5622 CA GLU C 149 99.873 −0.372 −0.221 1.00 41.17 C ATOM 5623 CB GLU C 149 100.532 0.535 −1.266 1.00 39.75 C ATOM 5624 CG GLU C 149 102.038 0.662 −1.083 1.00 39.00 C ATOM 5625 CD GLU C 149 102.703 1.461 −2.171 1.00 39.73 C ATOM 5626 OE1 GLU C 149 102.443 2.683 −2.265 1.00 39.67 C ATOM 5627 OE2 GLU C 149 103.490 0.868 −2.938 1.00 39.04 C ATOM 5628 C GLU C 149 100.183 0.120 1.195 1.00 44.52 C ATOM 5629 O GLU C 149 100.646 −0.656 2.032 1.00 44.69 C ATOM 5630 N GUI C 150 99.914 1.398 1.460 1.00 48.03 C ATOM 5631 CA GLU C 150 100.161 1.995 2.774 1.00 51.71 C ATOM 5632 CB GLU C 150 99.557 3.407 2.822 1.00 52.60 C ATOM 5633 CG GLU C 150 100.095 4.362 1.763 1.00 56.26 C ATOM 5634 CD GLU C 150 101.508 4.869 2.052 1.00 57.57 C ATOM 5635 OE1 GLU C 150 101.735 5.354 3.178 1.00 58.02 C ATOM 5636 OE2 GLU C 150 102.381 4.803 1.153 1.00 58.12 C ATOM 5637 C GLU C 150 99.603 1.136 3.938 1.00 53.38 C ATOM 5638 O GLU C 150 100.159 1.112 5.042 1.00 52.61 C ATOM 5639 N GLU C 151 98.515 0.420 3.677 1.00 55.17 C ATOM 5640 CA GLU C 151 97.891 −0.431 4.681 1.00 58.21 C ATOM 5641 CB GLU C 151 96.636 −1.087 4.097 1.00 60.47 C ATOM 5642 CG GLU C 151 95.349 −0.835 4.868 1.00 62.11 C ATOM 5643 CD GLU C 151 94.154 −1.512 4.222 1.00 63.63 C ATOM 5644 OE1 GLU C 151 94.025 −1.410 2.978 1.00 64.05 C ATOM 5645 OE2 GLU C 151 93.347 −2.135 4.955 1.00 63.74 C ATOM 5646 C GLU C 151 98.845 −1.519 5.182 1.00 59.56 C ATOM 5647 O GLU C 151 99.118 −1.609 6.375 1.00 60.86 C ATOM 5648 N ALA C 152 99.345 −2.346 4.269 1.00 60.60 C ATOM 5649 CA ALA C 152 100.263 −3.422 4.626 1.00 61.88 C ATOM 5650 CB ALA C 152 100.455 −4.356 3.439 1.00 61.89 C ATOM 5651 C ALA C 152 101.616 −2.881 5.080 1.00 62.64 C ATOM 5652 O ALA C 152 102.398 −3.589 5.699 1.00 62.91 C ATOM 5653 N ALA C 153 101.888 −1.622 4.769 1.00 64.35 C ATOM 5654 CA ALA C 153 103.146 −1.005 5.144 1.00 66.65 C ATOM 5655 CB ALA C 153 103.441 0.166 4.222 1.00 66.57 C ATOM 5656 C ALA C 153 103.114 −0.534 6.593 1.00 68.35 C ATOM 5657 O ALA C 153 104.159 −0.238 7.177 1.00 67.40 C ATOM 5658 N ILE C 154 101.913 −0.463 7.167 1.00 70.84 C ATOM 5659 CA ILE C 154 101.753 −0.021 8.549 1.00 73.04 C ATOM 5660 CB ILE C 154 100.276 0.333 8.874 1.00 72.44 C ATOM 5661 CG2 ILE C 154 100.160 0.823 10.308 0.00 73.15 C ATOM 5662 CG1 ILE C 154 99.768 1.405 7.906 0.00 73.18 C ATOM 5663 CD1 ILE C 154 100.596 2.681 7.891 0.00 73.32 C ATOM 5664 C ILE C 154 102.242 −1.083 9.530 1.00 74.39 C ATOM 5665 O ILE C 154 103.164 −0.836 10.314 1.00 75.10 C ATOM 5666 N ARG C 155 101.638 −2.267 9.481 1.00 75.33 C ATOM 5667 CA ARG C 155 102.035 −3.343 10.386 1.00 77.14 C ATOM 5668 CB ARG C 155 101.354 −4.655 9.970 1.00 77.56 C ATOM 5669 CG ARG C 155 101.473 −4.969 8.491 1.00 79.06 C ATOM 5670 CD ARG C 155 100.453 −6.012 8.042 1.00 79.84 C ATOM 5671 NE ARG C 155 101.032 −7.346 7.880 1.00 82.03 C ATOM 5672 CZ ARG C 155 101.458 −8.120 8.876 1.00 83.21 C ATOM 5673 NH1 ARG C 155 101.376 −7.702 10.130 1.00 83.46 C ATOM 5674 NH2 ARG C 155 101.967 −9.320 8.617 1.00 83.34 C ATOM 5675 C ARG C 155 103.557 −3.521 10.429 1.00 77.49 C ATOM 5676 O ARG C 155 104.141 −3.689 11.505 1.00 76.81 C ATOM 5677 N ARG C 156 104.185 −3.454 9.256 1.00 78.72 C ATOM 5678 CA ARG C 156 105.631 −3.611 9.120 1.00 80.26 C ATOM 5679 CB ARG C 156 106.371 −2.543 9.936 1.00 79.66 C ATOM 5680 CG ARG C 156 106.197 −1.128 9.442 1.00 78.84 C ATOM 5681 CD ARG C 156 106.951 −0.151 10.332 1.00 78.63 C ATOM 5682 NE ARG C 156 106.958 1.201 9.777 1.00 79.37 C ATOM 5683 CZ ARG C 156 107.560 2.243 10.344 1.00 79.78 C ATOM 5684 NH1 ARG C 156 108.210 2.098 11.492 1.00 80.21 C ATOM 5685 NH2 ARG C 156 107.513 3.434 9.763 1.00 79.89 C ATOM 5686 C ARG C 156 106.075 −4.997 9.586 1.00 81.59 C ATOM 5687 O ARG C 156 106.298 −5.862 8.715 0.00 81.82 C ATOM 5688 OXT ARG C 156 106.182 −5.207 10.817 1.00 83.28 C ATOM 5689 CB LEU D 270 75.377 10.305 15.206 1.00 63.79 D ATOM 5690 CG LEU D 270 75.038 9.447 13.983 1.00 64.88 D ATOM 5691 CD1 LEU D 270 73.550 9.589 13.707 1.00 64.89 D ATOM 5692 CD2 LEU D 270 75.842 9.894 12.762 1.00 64.87 D ATOM 5693 C LEU D 270 77.526 9.458 16.216 1.00 61.89 D ATOM 5694 O LEU D 270 78.274 9.273 17.176 1.00 61.69 D ATOM 5695 N LEU D 270 75.776 10.456 17.643 1.00 62.12 D ATOM 5696 CA LEU D 270 76.015 9.627 16.425 1.00 62.72 D ATOM 5697 N LYS D 271 77.975 9.523 14.966 1.00 60.94 D ATOM 5698 CA LYS D 271 79.394 9.377 14.666 1.00 59.23 D ATOM 5699 CB LYS D 271 79.635 9.177 13.157 1.00 61.06 D ATOM 5700 CG LYS D 271 79.243 10.362 12.273 1.00 61.84 D ATOM 5701 CD LYS D 271 79.810 10.233 10.859 1.00 62.36 D ATOM 5702 CE LYS D 271 81.303 10.589 10.782 1.00 63.95 D ATOM 5703 NZ LYS D 271 82.195 9.772 11.664 1.00 62.34 D ATOM 5704 C LYS D 271 80.146 10.607 15.114 1.00 56.61 D ATOM 5705 O LYS D 271 79.604 11.715 15.119 1.00 56.97 D ATOM 5706 N ARG D 272 81.403 10.412 15.483 1.00 53.78 D ATOM 5707 CA ARG D 272 82.212 11.531 15.902 1.00 51.25 D ATOM 5708 CB ARG D 272 81.625 12.153 17.159 1.00 50.62 D ATOM 5709 CG ARG D 272 81.295 13.617 16.977 1.00 50.35 D ATOM 5710 CD ARG D 272 82.497 14.465 17.304 1.00 50.29 D ATOM 5711 NE ARG D 272 82.835 15.461 16.290 1.00 50.91 D ATOM 5712 CZ ARG D 272 82.084 16.507 15.950 1.00 50.34 D ATOM 5713 NH1 ARG D 272 80.913 16.720 16.528 1.00 50.37 D ATOM 5714 NH2 ARG D 272 82.528 17.376 15.049 1.00 50.67 D ATOM 5715 C ARG D 272 83.652 11.142 16.124 1.00 49.27 D ATOM 5716 O ARG D 272 83.995 10.497 17.112 1.00 50.77 D ATOM 5717 N ASP D 273 84.498 11.523 15.180 1.00 45.44 D ATOM 5718 CA ASP D 273 85.904 11.229 15.310 1.00 40.81 D ATOM 5719 CB ASP D 273 86.582 11.281 13.951 1.00 40.44 D ATOM 5720 CG ASP D 273 87.998 10.765 13.997 1.00 40.32 D ATOM 5721 OD1 ASP D 273 88.731 11.138 14.939 1.00 40.48 D ATOM 5722 OD2 ASP D 273 88.377 9.991 13.094 1.00 40.70 D ATOM 5723 C ASP D 273 86.486 12.295 16.231 1.00 38.02 D ATOM 5724 O ASP D 273 87.082 13.269 15.771 1.00 36.97 D ATOM 5725 N LEU D 274 86.301 12.096 17.536 1.00 35.35 D ATOM 5726 CA LEU D 274 86.783 13.026 18.562 1.00 32.44 D ATOM 5727 CB LEU D 274 86.596 12.405 19.957 1.00 32.29 D ATOM 5728 CG LEU D 274 85.237 11.729 20.146 1.00 33.44 D ATOM 5729 CD1 LEU D 274 85.148 10.949 21.454 1.00 33.06 D ATOM 5730 CD2 LEU D 274 84.185 12.796 20.076 1.00 33.99 D ATOM 5731 C LEU D 274 88.250 13.443 18.376 1.00 30.29 D ATOM 5732 O LEU D 274 88.589 14.620 18.487 1.00 29.35 D ATOM 5733 N ILE D 275 89.119 12.481 18.090 1.00 27.97 D ATOM 5734 CA ILE D 275 90.529 12.790 17.919 1.00 26.53 D ATOM 5735 CB ILE D 275 91.366 11.487 17.721 1.00 26.41 D ATOM 5736 CG2 ILE D 275 92.798 11.829 17.316 1.00 25.43 D ATOM 5737 CG1 ILE D 275 91.390 10.679 19.029 1.00 24.46 D ATOM 5738 CD1 ILE D 275 92.026 11.404 20.207 1.00 19.75 D ATOM 5739 C ILE D 275 90.738 13.764 16.748 1.00 26.48 D ATOM 5740 O ILE D 275 91.490 14.743 16.855 1.00 26.90 D ATOM 5741 N THR D 276 90.052 13.503 15.642 1.00 24.10 D ATOM 5742 CA THR D 276 90.134 14.348 14.469 1.00 22.65 D ATOM 5743 CB THR D 276 89.447 13.632 13.273 1.00 21.40 D ATOM 5744 OG1 THR D 276 90.221 12.483 12.942 1.00 21.35 D ATOM 5745 CG2 THR D 276 89.321 14.528 12.052 1.00 18.26 D ATOM 5746 C THR D 276 89.477 15.711 14.769 1.00 23.50 D ATOM 5747 O THR D 276 90.041 16.768 14.462 1.00 22.31 D ATOM 5748 N SER D 277 88.305 15.673 15.397 1.00 23.60 D ATOM 5749 CA SER D 277 87.582 16.883 15.745 1.00 25.64 D ATOM 5750 CB SER D 277 86.156 16.544 16.144 1.00 25.38 D ATOM 5751 OG SER D 277 85.440 16.087 15.019 1.00 27.48 D ATOM 5752 C SER D 277 88.215 17.739 16.837 1.00 26.65 D ATOM 5753 O SER D 277 88.380 18.939 16.657 1.00 29.61 D ATOM 5754 N LEU D 278 88.561 17.147 17.970 1.00 25.91 D ATOM 5755 CA LEU D 278 89.180 17.922 19.035 1.00 26.38 D ATOM 5756 CB LEU D 278 89.564 17.027 20.218 1.00 26.10 D ATOM 5757 CG LEU D 278 88.426 16.811 21.194 1.00 24.98 D ATOM 5758 CD1 LEU D 278 88.017 18.153 21.792 1.00 26.21 D ATOM 5759 CD2 LEU D 278 87.257 16.190 20.458 1.00 28.73 D ATOM 5760 C LEU D 278 90.426 18.621 18.530 1.00 26.46 D ATOM 5761 O LEU D 278 91.038 18.189 17.549 1.00 27.90 D ATOM 5762 N PRO D 279 90.803 19.733 19.177 1.00 26.62 D ATOM 5763 CD PRO D 279 89.970 20.521 20.096 1.00 26.92 D ATOM 5764 CA PRO D 279 91.994 20.496 18.799 1.00 27.49 D ATOM 5765 CB PRO D 279 91.940 21.686 19.739 1.00 26.12 D ATOM 5766 CG PRO D 279 90.495 21.922 19.861 1.00 25.59 D ATOM 5767 C PRO D 279 93.212 19.620 19.047 1.00 29.22 D ATOM 5768 O PRO D 279 93.221 18.827 19.991 1.00 30.55 D ATOM 5769 N PHE D 280 94.234 19.775 18.210 1.00 29.38 D ATOM 5770 CA PHE D 280 95.452 18.980 18.303 1.00 29.08 D ATOM 5771 CB PHE D 280 96.567 19.668 17.518 1.00 30.38 D ATOM 5772 CG PHE D 280 97.839 18.871 17.438 1.00 33.85 D ATOM 5773 CD1 PHE D 280 97.849 17.585 16.890 1.00 35.64 D ATOM 5774 CD2 PHE D 280 99.038 19.415 17.886 1.00 34.62 D ATOM 5775 CE1 PHE D 280 99.045 16.852 16.789 1.00 36.28 D ATOM 5776 CE2 PHE D 280 100.237 18.696 17.790 1.00 35.86 D ATOM 5777 CZ PHE D 280 100.242 17.410 17.239 1.00 36.27 D ATOM 5778 C PHE D 280 95.883 18.747 19.746 1.00 28.87 D ATOM 5779 O PHE D 280 96.100 17.611 20.167 1.00 28.22 D ATOM 5780 N GLU D 281 95.977 19.824 20.513 1.00 29.70 D ATOM 5781 CA GLU D 281 96.394 19.735 21.906 1.00 30.73 D ATOM 5782 CB GLU D 281 96.367 21.124 22.544 1.00 30.74 D ATOM 5783 CG GLU D 281 96.958 22.225 21.686 1.00 35.82 D ATOM 5784 CD GLU D 281 96.181 22.455 20.365 1.00 39.11 D ATOM 5785 OE1 GLU D 281 94.927 22.371 20.364 1.00 37.33 D ATOM 5786 OE2 GLU D 281 96.838 22.734 19.329 1.00 41.78 D ATOM 5787 C GLU D 281 95.508 18.767 22.707 1.00 30.47 D ATOM 5788 O GLU D 281 95.998 17.800 23.291 1.00 29.60 D ATOM 5789 N ILE D 282 94.200 19.006 22.731 1.00 30.62 D ATOM 5790 CA ILE D 282 93.326 18.115 23.495 1.00 30.51 D ATOM 5791 CB ILE D 282 91.826 18.479 23.367 1.00 28.68 D ATOM 5792 CG2 ILE D 282 90.973 17.454 24.096 1.00 25.40 D ATOM 5793 CG1 ILE D 282 91.559 19.841 24.002 1.00 28.37 D ATOM 5794 CD1 ILE D 282 92.338 20.960 23.374 1.00 29.50 D ATOM 5795 C ILE D 282 93.506 16.667 23.085 1.00 30.93 D ATOM 5796 O ILE D 282 93.569 15.798 23.939 1.00 32.03 D ATOM 5797 N SER D 283 93.597 16.403 21.786 1.00 33.38 D ATOM 5798 CA SER D 283 93.773 15.037 21.315 1.00 33.57 D ATOM 5799 CB SER D 283 93.729 14.991 19.793 1.00 33.09 D ATOM 5800 OG SER D 283 92.440 14.625 19.343 1.00 33.69 D ATOM 5801 C SER D 283 95.060 14.383 21.806 1.00 34.43 D ATOM 5802 O SER D 283 95.102 13.171 21.996 1.00 35.71 D ATOM 5803 N LEU D 284 96.121 15.158 21.996 1.00 33.67 D ATOM 5804 CA LEU D 284 97.345 14.541 22.479 1.00 33.99 D ATOM 5805 CB LEU D 284 98.511 15.514 22.412 1.00 34.78 D ATOM 5806 CG LEU D 284 98.908 15.828 20.966 1.00 37.92 D ATOM 5807 CD1 LEU D 284 99.965 16.921 20.972 1.00 38.44 D ATOM 5808 CD2 LEU D 284 99.424 14.571 20.264 1.00 35.81 D ATOM 5809 C LEU D 284 97.105 14.089 23.908 1.00 34.14 D ATOM 5810 O LEU D 284 97.469 12.972 24.268 1.00 35.96 D ATOM 5811 N LYS D 285 96.470 14.944 24.710 1.00 32.83 D ATOM 5812 CA LYS D 285 96.180 14.598 26.094 1.00 31.02 D ATOM 5813 CB LYS D 285 95.192 15.590 26.711 1.00 32.29 D ATOM 5814 CG LYS D 285 95.694 17.027 26.672 1.00 34.86 D ATOM 5815 CD LYS D 285 94.977 17.944 27.659 1.00 38.81 D ATOM 5816 CE LYS D 285 95.626 17.931 29.043 1.00 41.32 D ATOM 5817 NZ LYS D 285 95.083 19.055 29.866 1.00 43.73 D ATOM 5818 C LYS D 285 95.603 13.194 26.129 1.00 28.79 D ATOM 5819 O LYS D 285 96.124 12.305 26.823 1.00 29.62 D ATOM 5820 N ILE D 286 94.538 12.991 25.360 1.00 25.19 D ATOM 5821 CA ILE D 286 93.898 11.681 25.281 1.00 24.05 D ATOM 5822 CB ILE D 286 92.834 11.660 24.148 1.00 22.82 D ATOM 5823 CG2 ILE D 286 92.176 10.291 24.060 1.00 21.24 D ATOM 5824 CG1 ILE D 286 91.800 12.757 24.414 1.00 23.94 D ATOM 5825 CD1 ILE D 286 90.731 12.886 23.321 1.00 23.24 D ATOM 5826 C ILE D 286 94.950 10.583 25.036 1.00 23.79 D ATOM 5827 O ILE D 286 94.970 9.573 25.738 1.00 22.04 D ATOM 5828 N PHE D 287 95.825 10.788 24.051 1.00 21.07 D ATOM 5829 CA PHE D 287 96.844 9.790 23.746 1.00 21.11 D ATOM 5830 CB PHE D 287 97.596 10.147 22.469 1.00 20.53 D ATOM 5831 CG PHE D 287 96.842 9.818 21.221 1.00 20.94 D ATOM 5832 CD1 PHE D 287 96.528 8.495 20.915 1.00 18.61 D ATOM 5833 CD2 PHE D 287 96.445 10.831 20.340 1.00 20.85 D ATOM 5834 CE1 PHE D 287 95.835 8.184 19.754 1.00 17.26 D ATOM 5835 CE2 PHE D 287 95.752 10.525 19.177 1.00 18.21 D ATOM 5836 CZ PHE D 287 95.444 9.204 18.876 1.00 16.07 D ATOM 5837 C PHE D 287 97.849 9.539 24.859 1.00 21.96 D ATOM 5838 O PHE D 287 98.314 8.418 25.035 1.00 20.26 D ATOM 5839 N ASN D 288 98.182 10.592 25.593 1.00 23.06 D ATOM 5840 CA ASN D 288 99.128 10.494 26.677 1.00 25.24 D ATOM 5841 CB ASN D 288 99.598 11.892 27.089 1.00 25.50 D ATOM 5842 CG ASN D 288 100.691 12.432 26.166 1.00 27.45 D ATOM 5843 OD1 ASN D 288 101.539 11.660 25.680 1.00 29.10 D ATOM 5844 ND2 ASN D 288 100.696 13.750 25.936 1.00 25.61 D ATOM 5845 C ASN D 288 98.585 9.695 27.883 1.00 28.89 D ATOM 5846 O ASN D 288 99.331 9.376 28.815 1.00 28.16 D ATOM 5847 N TYR D 289 97.289 9.368 27.846 1.00 30.81 D ATOM 5848 CA TYR D 289 96.633 8.560 28.879 1.00 33.41 D ATOM 5849 CB TYR D 289 95.210 9.038 29.193 1.00 35.09 D ATOM 5850 CG TYR D 289 95.100 10.237 30.098 1.00 38.19 D ATOM 5851 CD1 TYR D 289 95.713 10.256 31.343 1.00 37.23 D ATOM 5852 CE1 TYR D 289 95.585 11.353 32.182 1.00 37.83 D ATOM 5853 CD2 TYR D 289 94.353 11.348 29.713 1.00 38.71 D ATOM 5854 CE2 TYR D 289 94.219 12.447 30.543 1.00 39.19 D ATOM 5855 CZ TYR D 289 94.838 12.449 31.778 1.00 38.07 D ATOM 5856 OH TYR D 289 94.716 13.558 32.596 1.00 37.65 D ATOM 5857 C TYR D 289 96.496 7.129 28.375 1.00 34.42 D ATOM 5858 O TYR D 289 95.852 6.288 29.016 1.00 34.85 D ATOM 5859 N LEU D 290 97.076 6.857 27.215 1.00 34.95 D ATOM 5860 CA LEU D 290 96.980 5.530 26.632 1.00 36.71 D ATOM 5861 CB LEU D 290 96.488 5.621 25.189 1.00 37.91 D ATOM 5862 CG LEU D 290 95.004 5.925 24.991 1.00 38.82 D ATOM 5863 CD1 LEU D 290 94.740 6.136 23.516 1.00 39.93 D ATOM 5864 CD2 LEU D 290 94.159 4.764 25.535 1.00 37.72 D ATOM 5865 C LEU D 290 98.302 4.802 26.664 1.00 37.19 D ATOM 5866 O LEU D 290 99.354 5.419 26.628 1.00 37.91 D ATOM 5867 N GLN D 291 98.256 3.482 26.744 1.00 38.53 D ATOM 5868 CA GLN D 291 99.493 2.736 26.771 1.00 39.34 D ATOM 5869 CB GLN D 291 99.251 1.308 27.236 1.00 40.51 D ATOM 5870 CG GLN D 291 98.786 1.213 28.657 1.00 43.34 D ATOM 5871 CD GLN D 291 98.666 −0.215 29.102 1.00 46.99 D ATOM 5872 OE1 GLN D 291 99.662 −0.945 29.172 1.00 50.86 D ATOM 5873 NE2 GLN D 291 97.444 −0.638 29.398 1.00 49.26 D ATOM 5874 C GLN D 291 100.090 2.749 25.374 1.00 38.68 D ATOM 5875 O GLN D 291 99.393 2.990 24.383 1.00 39.01 D ATOM 5876 N PHE D 292 101.386 2.482 25.308 1.00 35.62 D ATOM 5877 CA PHE D 292 102.096 2.492 24.059 1.00 32.95 D ATOM 5878 CB PHE D 292 103.583 2.209 24.335 1.00 32.02 D ATOM 5879 CG PHE D 292 104.010 0.795 24.109 1.00 29.67 D ATOM 5880 CD1 PHE D 292 104.290 0.349 22.829 1.00 30.05 D ATOM 5881 CD2 PHE D 292 104.221 −0.064 25.176 1.00 29.27 D ATOM 5882 CE1 PHE D 292 104.788 −0.932 22.613 1.00 30.66 D ATOM 5883 CE2 PHE D 292 104.719 −1.348 24.972 1.00 29.01 D ATOM 5884 CZ PHE D 292 105.004 −1.781 23.686 1.00 29.86 D ATOM 5885 C PHE D 292 101.477 1.552 23.035 1.00 32.44 D ATOM 5886 O PHE D 292 101.384 1.894 21.852 1.00 33.62 D ATOM 5887 N GLU D 293 101.018 0.389 23.481 1.00 31.32 D ATOM 5888 CA GLU D 293 100.396 −0.551 22.560 1.00 29.89 D ATOM 5889 CB GLU D 293 99.974 −1.819 23.296 1.00 29.10 D ATOM 5890 CG GLU D 293 101.135 −2.712 23.586 1.00 30.44 D ATOM 5891 CD GLU D 293 101.534 −2.717 25.053 1.00 31.93 D ATOM 5892 OE1 GLU D 293 101.473 −1.647 25.722 1.00 28.98 D ATOM 5893 OE2 GLU D 293 101.924 −3.815 25.518 1.00 32.42 D ATOM 5894 C GLU D 293 99.187 0.044 21.864 1.00 28.52 D ATOM 5895 O GLU D 293 98.978 −0.193 20.679 1.00 26.63 D ATOM 5896 N ASP D 294 98.391 0.802 22.615 1.00 29.50 D ATOM 5897 CA ASP D 294 97.193 1.431 22.081 1.00 30.32 D ATOM 5898 CB ASP D 294 96.330 2.030 23.210 1.00 32.63 D ATOM 5899 CG ASP D 294 95.768 0.968 24.183 1.00 36.82 D ATOM 5900 OD1 ASP D 294 95.503 −0.192 23.772 1.00 39.44 D ATOM 5901 OD2 ASP D 294 95.563 1.309 25.369 1.00 38.44 D ATOM 5902 C ASP D 294 97.585 2.542 21.103 1.00 29.40 D ATOM 5903 O ASP D 294 96.796 2.930 20.245 1.00 27.84 D ATOM 5904 N ILE D 295 98.805 3.050 21.237 1.00 28.17 D ATOM 5905 CA ILE D 295 99.266 4.114 20.362 1.00 28.34 D ATOM 5906 CB ILE D 295 100.510 4.784 20.917 1.00 28.05 D ATOM 5907 CG2 ILE D 295 100.845 5.998 20.077 1.00 25.51 D ATOM 5908 CG1 ILE D 295 100.294 5.145 22.392 1.00 30.16 D ATOM 5909 CD1 ILE D 295 99.338 6.283 22.658 1.00 31.34 D ATOM 5910 C ILE D 295 99.605 3.549 18.990 1.00 28.98 D ATOM 5911 O ILE D 295 99.310 4.151 17.956 1.00 28.75 D ATOM 5912 N ILE D 296 100.227 2.381 18.996 1.00 29.17 D ATOM 5913 CA ILE D 296 100.612 1.715 17.768 1.00 30.36 D ATOM 5914 CB ILE D 296 101.521 0.491 18.085 1.00 30.31 D ATOM 5915 CG2 ILE D 296 101.236 −0.660 17.148 1.00 28.53 D ATOM 5916 CG1 ILE D 296 102.987 0.911 17.989 1.00 31.04 D ATOM 5917 CD1 ILE D 296 103.353 2.115 18.829 1.00 32.07 D ATOM 5918 C ILE D 296 99.379 1.308 16.965 1.00 30.74 D ATOM 5919 O ILE D 296 99.376 1.398 15.741 1.00 30.48 D ATOM 5920 N ASN D 297 98.330 0.865 17.642 1.00 31.12 D ATOM 5921 CA ASN D 297 97.121 0.506 16.924 1.00 33.08 D ATOM 5922 CB ASN D 297 96.096 −0.099 17.865 1.00 33.38 D ATOM 5923 CG ASN D 297 96.393 −1.537 18.171 1.00 37.25 D ATOM 5924 OD1 ASN D 297 95.953 −2.067 19.194 1.00 37.85 D ATOM 5925 ND2 ASN D 297 97.143 −2.196 17.270 1.00 37.30 D ATOM 5926 C ASN D 297 96.548 1.767 16.316 1.00 33.81 D ATOM 5927 O ASN D 297 96.220 1.817 15.123 1.00 34.30 D ATOM 5928 N SER D 298 96.435 2.780 17.168 1.00 32.14 D ATOM 5929 CA SER D 298 95.912 4.079 16.792 1.00 30.45 D ATOM 5930 CB SER D 298 96.100 5.073 17.939 1.00 29.96 D ATOM 5931 OG SER D 298 95.395 4.648 19.087 1.00 27.42 D ATOM 5932 C SER D 298 96.656 4.566 15.583 1.00 30.58 D ATOM 5933 O SER D 298 96.103 5.255 14.731 1.00 32.34 D ATOM 5934 N LEU D 299 97.930 4.216 15.514 1.00 29.49 D ATOM 5935 CA LEU D 299 98.738 4.628 14.387 1.00 28.00 D ATOM 5936 CB LEU D 299 100.164 4.131 14.570 1.00 28.12 D ATOM 5937 CG LEU D 299 101.291 5.098 14.240 1.00 28.83 D ATOM 5938 CD1 LEU D 299 101.105 6.442 14.938 1.00 28.49 D ATOM 5939 CD2 LEU D 299 102.595 4.455 14.703 1.00 30.72 D ATOM 5940 C LEU D 299 98.147 4.063 13.108 1.00 27.04 D ATOM 5941 O LEU D 299 98.382 4.608 12.045 1.00 28.76 D ATOM 5942 N GLY D 300 97.356 2.996 13.212 1.00 25.60 D ATOM 5943 CA GLY D 300 96.783 2.387 12.018 1.00 25.16 D ATOM 5944 C GLY D 300 95.268 2.423 11.857 1.00 25.49 D ATOM 5945 O GLY D 300 94.665 1.528 11.258 1.00 24.96 D ATOM 5946 N VAL D 301 94.661 3.476 12.381 1.00 26.14 D ATOM 5947 CA VAL D 301 93.223 3.677 12.335 1.00 25.65 D ATOM 5948 CB VAL D 301 92.783 4.425 13.635 1.00 25.13 D ATOM 5949 CG1 VAL D 301 91.377 4.975 13.523 1.00 23.49 D ATOM 5950 CG2 VAL D 301 92.881 3.470 14.818 1.00 25.09 D ATOM 5951 C VAL D 301 92.853 4.482 11.085 1.00 26.83 D ATOM 5952 O VAL D 301 91.895 4.160 10.386 1.00 29.06 D ATOM 5953 N SER D 302 93.624 5.517 10.781 1.00 27.15 D ATOM 5954 CA SER D 302 93.321 6.327 9.611 1.00 27.14 D ATOM 5955 CB SER D 302 92.021 7.096 9.832 1.00 26.96 D ATOM 5956 OG SER D 302 92.186 8.048 10.876 1.00 28.29 D ATOM 5957 C SER D 302 94.442 7.308 9.329 1.00 26.93 D ATOM 5958 O SER D 302 95.174 7.696 10.239 1.00 27.64 D ATOM 5959 N GLN D 303 94.558 7.720 8.067 1.00 26.82 D ATOM 5960 CA GLN D 303 95.596 8.658 7.661 1.00 25.04 D ATOM 5961 CB GLN D 303 95.362 9.166 6.244 1.00 23.83 D ATOM 5962 CG GLN D 303 95.865 8.261 5.154 1.00 29.99 D ATOM 5963 CD GLN D 303 97.398 8.160 5.090 1.00 32.84 D ATOM 5964 OE1 GLN D 303 97.942 7.457 4.239 1.00 34.49 D ATOM 5965 NE2 GLN D 303 98.091 8.863 5.986 1.00 36.06 D ATOM 5966 C GLN D 303 95.653 9.852 8.587 1.00 23.97 D ATOM 5967 O GLN D 303 96.743 10.343 8.901 1.00 22.53 D ATOM 5968 N ASN D 304 94.490 10.322 9.034 1.00 22.85 D ATOM 5969 CA ASN D 304 94.479 11.487 9.908 1.00 24.54 D ATOM 5970 CB ASN D 304 93.082 12.042 10.095 1.00 25.34 D ATOM 5971 CG ASN D 304 93.105 13.358 10.814 1.00 28.24 D ATOM 5972 OD1 ASN D 304 92.215 13.657 11.613 1.00 30.04 D ATOM 5973 ND2 ASN D 304 94.143 14.163 10.544 1.00 29.46 D ATOM 5974 C ASN D 304 95.058 11.172 11.270 1.00 25.25 D ATOM 5975 O ASN D 304 95.876 11.928 11.820 1.00 24.93 D ATOM 5976 N TRP D 305 94.609 10.063 11.835 1.00 25.15 D ATOM 5977 CA TRP D 305 95.139 9.658 13.118 1.00 25.51 D ATOM 5978 CB TRP D 305 94.447 8.373 13.587 1.00 25.43 D ATOM 5979 CG TRP D 305 93.138 8.630 14.311 1.00 26.00 D ATOM 5980 CD2 TRP D 305 92.614 7.880 15.410 1.00 26.49 D ATOM 5981 CE2 TRP D 305 91.351 8.425 15.730 1.00 24.97 D ATOM 5982 CE3 TRP D 305 93.090 6.796 16.157 1.00 27.62 D ATOM 5983 CD1 TRP D 305 92.199 9.581 14.015 1.00 25.09 D ATOM 5984 NE1 TRP D 305 91.122 9.461 14.864 1.00 24.10 D ATOM 5985 CZ2 TRP D 305 90.559 7.918 16.764 1.00 23.76 D ATOM 5986 CZ3 TRP D 305 92.299 6.297 17.183 1.00 25.00 D ATOM 5987 CH2 TRP D 305 91.053 6.859 17.474 1.00 24.03 D ATOM 5988 C TRP D 305 96.656 9.477 12.935 1.00 24.69 D ATOM 5989 O TRP D 305 97.445 9.992 13.734 1.00 25.68 D ATOM 5990 N ASN D 306 97.054 8.786 11.863 1.00 22.23 D ATOM 5991 CA ASN D 306 98.471 8.583 11.555 1.00 21.36 D ATOM 5992 CB ASN D 306 98.669 7.946 10.182 1.00 19.88 D ATOM 5993 CG ASN D 306 100.134 7.572 9.920 1.00 20.62 D ATOM 5994 OD1 ASN D 306 100.608 6.526 10.394 1.00 21.63 D ATOM 5995 ND2 ASN D 306 100.860 8.427 9.176 1.00 16.92 D ATOM 5996 C ASN D 306 99.203 9.913 11.517 1.00 21.93 D ATOM 5997 O ASN D 306 100.356 10.009 11.912 1.00 21.70 D ATOM 5998 N LYS D 307 98.533 10.930 11.000 1.00 22.01 D ATOM 5999 CA LYS D 307 99.134 12.235 10.907 1.00 23.12 D ATOM 6000 CB LYS D 307 98.270 13.136 10.027 1.00 24.42 D ATOM 6001 CG LYS D 307 98.897 14.469 9.657 1.00 25.07 D ATOM 6002 CD LYS D 307 97.803 15.504 9.446 1.00 29.41 D ATOM 6003 CE LYS D 307 98.290 16.723 8.650 1.00 31.20 D ATOM 6004 NZ LYS D 307 98.710 16.351 7.251 1.00 30.25 D ATOM 6005 C LYS D 307 99.298 12.868 12.284 1.00 24.28 D ATOM 6006 O LYS D 307 100.387 13.292 12.654 1.00 26.10 D ATOM 6007 N ILE D 308 98.214 12.902 13.047 1.00 23.74 D ATOM 6008 CA ILE D 308 98.217 13.520 14.359 1.00 25.31 D ATOM 6009 CB ILE D 308 96.843 13.350 15.042 1.00 27.23 D ATOM 6010 CG2 ILE D 308 96.899 13.810 16.475 1.00 27.28 D ATOM 6011 CG1 ILE D 308 95.794 14.187 14.294 1.00 28.70 D ATOM 6012 CD1 ILE D 308 94.383 14.048 14.808 1.00 26.95 D ATOM 6013 C ILE D 308 99.298 13.018 15.292 1.00 25.96 D ATOM 6014 O ILE D 308 100.079 13.797 15.838 1.00 24.81 D ATOM 6015 N ILE D 309 99.353 11.710 15.464 1.00 26.12 D ATOM 6016 CA ILE D 309 100.314 11.115 16.359 1.00 25.75 D ATOM 6017 CB ILE D 309 99.990 9.603 16.538 1.00 25.30 D ATOM 6018 CG2 ILE D 309 100.995 8.937 17.437 1.00 24.21 D ATOM 6019 CG1 ILE D 309 98.617 9.437 17.181 1.00 21.52 D ATOM 6020 CD1 ILE D 309 98.160 8.023 17.261 1.00 23.28 D ATOM 6021 C ILE D 309 101.755 11.313 15.906 1.00 26.74 D ATOM 6022 O ILE D 309 102.626 11.586 16.729 1.00 27.84 D ATOM 6023 N ARG D 310 102.026 11.177 14.610 1.00 28.38 D ATOM 6024 CA ARG D 310 103.401 11.350 14.098 1.00 29.18 D ATOM 6025 CB ARG D 310 103.513 10.811 12.663 1.00 28.52 D ATOM 6026 CG ARG D 310 103.531 9.277 12.560 1.00 30.67 D ATOM 6027 CD ARG D 310 103.052 8.787 11.186 1.00 34.25 D ATOM 6028 NE ARG D 310 104.098 8.252 10.323 1.00 36.16 D ATOM 6029 CZ ARG D 310 105.097 8.969 9.827 1.00 38.55 D ATOM 6030 NH1 ARG D 310 105.200 10.259 10.095 1.00 42.20 D ATOM 6031 NH2 ARG D 310 106.009 8.391 9.069 1.00 41.89 D ATOM 6032 C ARG D 310 103.838 12.811 14.139 1.00 28.88 D ATOM 6033 O ARG D 310 104.996 13.133 13.873 1.00 28.32 D ATOM 6034 N LYS D 311 102.900 13.681 14.496 1.00 29.76 D ATOM 6035 CA LYS D 311 103.172 15.104 14.570 1.00 32.11 D ATOM 6036 CB LYS D 311 101.894 15.868 14.227 1.00 32.03 D ATOM 6037 CG LYS D 311 102.061 17.362 14.098 1.00 36.15 D ATOM 6038 CD LYS D 311 100.731 18.049 13.814 1.00 39.43 D ATOM 6039 CE LYS D 311 100.895 19.580 13.814 1.00 42.31 D ATOM 6040 NZ LYS D 311 100.575 20.231 15.122 1.00 42.00 D ATOM 6041 C LYS D 311 103.728 15.564 15.934 1.00 32.85 D ATOM 6042 O LYS D 311 104.467 16.545 15.992 1.00 32.33 D ATOM 6043 N SER D 312 103.395 14.855 17.017 1.00 33.76 D ATOM 6044 CA SER D 312 103.857 15.223 18.365 1.00 33.60 D ATOM 6045 CB SER D 312 102.835 14.787 19.421 1.00 35.34 D ATOM 6046 OG SER D 312 103.198 15.271 20.712 1.00 39.47 D ATOM 6047 C SER D 312 105.222 14.667 18.781 1.00 31.68 D ATOM 6048 O SER D 312 105.456 13.468 18.728 1.00 32.40 D ATOM 6049 N THR D 313 106.125 15.543 19.198 1.00 30.17 D ATOM 6050 CA THR D 313 107.429 15.095 19.651 1.00 29.28 D ATOM 6051 CB THR D 313 108.502 16.214 19.480 1.00 30.08 D ATOM 6052 OG1 THR D 313 109.122 16.072 18.199 1.00 31.16 D ATOM 6053 CG2 THR D 313 109.580 16.132 20.558 1.00 30.05 D ATOM 6054 C THR D 313 107.270 14.701 21.128 1.00 27.77 D ATOM 6055 O THR D 313 107.658 13.603 21.538 1.00 26.51 D ATOM 6056 N SER D 314 106.666 15.599 21.901 1.00 26.12 D ATOM 6057 CA SER D 314 106.420 15.370 23.311 1.00 26.42 D ATOM 6058 CB SER D 314 105.499 16.454 23.886 1.00 25.86 D ATOM 6059 OG SER D 314 104.133 16.191 23.589 1.00 25.20 D ATOM 6060 C SER D 314 105.755 14.011 23.534 1.00 26.86 D ATOM 6061 O SER D 314 106.064 13.314 24.486 1.00 27.19 D ATOM 6062 N LEU D 315 104.830 13.633 22.668 1.00 26.78 D ATOM 6063 CA LEU D 315 104.169 12.368 22.851 1.00 26.12 D ATOM 6064 CB LEU D 315 103.148 12.167 21.741 1.00 25.84 D ATOM 6065 CG LEU D 315 102.212 10.960 21.711 1.00 26.39 D ATOM 6066 CD1 LEU D 315 101.094 11.269 20.721 1.00 27.77 D ATOM 6067 CD2 LEU D 315 102.933 9.691 21.303 1.00 24.47 D ATOM 6068 C LEU D 315 105.186 11.229 22.899 1.00 26.05 D ATOM 6069 O LEU D 315 105.108 10.373 23.780 1.00 27.85 D ATOM 6070 N TRP D 316 106.165 11.224 21.998 1.00 24.50 D ATOM 6071 CA TRP D 316 107.141 10.138 22.011 1.00 25.89 D ATOM 6072 CB TRP D 316 107.751 9.952 20.607 1.00 24.16 D ATOM 6073 CG TRP D 316 106.708 9.452 19.635 1.00 21.27 D ATOM 6074 CD2 TRP D 316 106.177 8.123 19.565 1.00 18.61 D ATOM 6075 CE2 TRP D 316 105.107 8.146 18.646 1.00 18.90 D ATOM 6076 CE3 TRP D 316 106.498 6.917 20.193 1.00 20.19 D ATOM 6077 CD1 TRP D 316 105.959 10.206 18.767 1.00 20.28 D ATOM 6078 NE1 TRP D 316 104.994 9.428 18.177 1.00 19.42 D ATOM 6079 CZ2 TRP D 316 104.351 7.007 18.344 1.00 19.58 D ATOM 6080 CZ3 TRP D 316 105.741 5.778 19.892 1.00 21.16 D ATOM 6081 CH2 TRP D 316 104.682 5.835 18.975 1.00 20.34 D ATOM 6082 C TRP D 316 108.216 10.292 23.091 1.00 27.23 D ATOM 6083 O TRP D 316 108.854 9.311 23.519 1.00 27.64 D ATOM 6084 N LYS D 317 108.374 11.525 23.556 1.00 27.58 D ATOM 6085 CA LYS D 317 109.332 11.847 24.602 1.00 27.23 D ATOM 6086 CS LYS D 317 109.463 13.360 24.759 1.00 29.14 D ATOM 6087 CG LYS D 317 110.589 13.760 25.682 1.00 32.80 D ATOM 6088 CD LYS D 317 110.743 15.264 25.749 1.00 35.26 D ATOM 6089 CE LYS D 317 111.774 15.652 26.805 1.00 37.31 D ATOM 6090 NZ LYS D 317 111.793 17.120 27.068 1.00 37.03 D ATOM 6091 C LYS D 317 108.822 11.275 25.910 1.00 25.94 D ATOM 6092 O LYS D 317 109.570 10.685 26.689 1.00 25.94 D ATOM 6093 N LYS D 318 107.533 11.473 26.142 1.00 23.54 D ATOM 6094 CA LYS D 318 106.921 10.980 27.345 1.00 21.52 D ATOM 6095 CB LYS D 318 105.457 11.403 27.426 1.00 19.84 D ATOM 6096 CG LYS D 318 105.276 12.802 27.949 1.00 15.81 D ATOM 6097 CD LYS D 318 103.822 13.127 28.039 1.00 17.16 D ATOM 6098 CE LYS D 318 103.592 14.588 28.439 1.00 19.94 D ATOM 6099 NZ LYS D 318 104.446 15.524 27.676 1.00 22.18 D ATOM 6100 C LYS D 318 107.026 9.474 27.389 1.00 21.47 D ATOM 6101 O LYS D 318 107.353 8.890 28.423 1.00 22.72 D ATOM 6102 N LEU D 319 106.754 8.825 26.271 1.00 20.41 D ATOM 6103 CA LEU D 319 106.834 7.373 26.259 1.00 19.54 D ATOM 6104 CB LEU D 319 106.427 6.839 24.894 1.00 17.41 D ATOM 6105 CG LEU D 319 104.933 6.610 24.750 1.00 14.60 D ATOM 6106 CD1 LEU D 319 104.590 6.417 23.307 1.00 15.84 D ATOM 6107 CD2 LEU D 319 104.520 5.398 25.581 1.00 13.04 D ATOM 6108 C LEU D 319 108.232 6.901 26.605 1.00 19.33 D ATOM 6109 O LEU D 319 108.395 6.014 27.441 1.00 18.41 D ATOM 6110 N LEU D 320 109.239 7.493 25.961 1.00 20.82 D ATOM 6111 CA LEU D 320 110.624 7.099 26.217 1.00 21.24 D ATOM 6112 CB LEU D 320 111.589 7.926 25.344 1.00 17.94 D ATOM 6113 CG LEU D 320 111.710 7.492 23.869 1.00 18.89 D ATOM 6114 CD1 LEU D 320 112.467 8.533 23.030 1.00 16.82 D ATOM 6115 CD2 LEU D 320 112.402 6.158 23.797 1.00 15.44 D ATOM 6116 C LEU D 320 110.965 7.259 27.701 1.00 22.18 D ATOM 6117 O LEU D 320 111.574 6.383 28.310 1.00 23.23 D ATOM 6118 N ILE D 321 110.545 8.375 28.281 1.00 22.59 D ATOM 6119 CA ILE D 321 110.824 8.661 29.676 1.00 22.13 D ATOM 6120 CB ILE D 321 110.462 10.125 30.007 1.00 21.71 D ATOM 6121 CG2 ILE D 321 110.406 10.336 31.509 1.00 20.64 D ATOM 6122 CG1 ILE D 321 111.471 11.053 29.324 1.00 20.39 D ATOM 6123 CD1 ILE D 321 111.312 12.527 29.639 1.00 17.62 D ATOM 6124 C ILE D 321 110.112 7.729 30.641 1.00 21.87 D ATOM 6125 O ILE D 321 110.726 7.204 31.551 1.00 23.61 D ATOM 6126 N SER D 322 108.819 7.526 30.449 1.00 22.79 D ATOM 6127 CA SER D 322 108.082 6.663 31.345 1.00 23.92 D ATOM 6128 CB SER D 322 106.610 6.624 30.943 1.00 24.36 D ATOM 6129 OG SER D 322 106.464 6.398 29.554 1.00 28.99 D ATOM 6130 C SER D 322 108.668 5.256 31.377 1.00 25.68 D ATOM 6131 O SER D 322 108.780 4.660 32.440 1.00 27.76 D ATOM 6132 N GLU D 323 109.041 4.718 30.222 1.00 24.70 D ATOM 6133 CA GLU D 323 109.625 3.389 30.188 1.00 23.55 D ATOM 6134 CB GLU D 323 109.581 2.835 28.775 1.00 24.33 D ATOM 6135 CG GLU D 323 108.228 2.303 28.385 1.00 25.11 D ATOM 6136 CD GLU D 323 107.953 0.951 29.008 1.00 26.37 D ATOM 6137 OE1 GLU D 323 108.775 0.024 28.805 1.00 26.30 D ATOM 6138 OE2 GLU D 323 106.920 0.809 29.695 1.00 27.36 D ATOM 6139 C GLU D 323 111.059 3.448 30.678 1.00 23.31 D ATOM 6140 O GLU D 323 111.773 2.443 30.684 1.00 23.15 D ATOM 6141 N ASN D 324 111.467 4.644 31.091 1.00 22.23 D ATOM 6142 CA ASN D 324 112.812 4.891 31.592 1.00 22.59 D ATOM 6143 CB ASN D 324 113.038 4.090 32.877 1.00 22.90 D ATOM 6144 CG ASN D 324 111.864 4.200 33.858 1.00 26.71 D ATOM 6145 OD1 ASN D 324 111.346 5.294 34.109 1.00 25.11 D ATOM 6146 ND2 ASN D 324 111.450 3.056 34.430 1.00 28.34 D ATOM 6147 C ASN D 324 113.911 4.565 30.560 1.00 23.12 D ATOM 6148 O ASN D 324 114.971 4.031 30.914 1.00 23.08 D ATOM 6149 N PHE D 325 113.667 4.881 29.285 1.00 22.49 D ATOM 6150 CA PHE D 325 114.673 4.613 28.246 1.00 22.20 D ATOM 6151 CB PHE D 325 114.005 4.332 26.882 1.00 18.54 D ATOM 6152 CG PHE D 325 113.296 2.991 26.806 1.00 18.28 D ATOM 6153 CD1 PHE D 325 112.080 2.864 26.117 1.00 17.36 D ATOM 6154 CD2 PHE D 325 113.828 1.860 27.425 1.00 17.01 D ATOM 6155 CE1 PHE D 325 111.404 1.631 26.053 1.00 15.65 D ATOM 6156 CE2 PHE D 325 113.165 0.617 27.369 1.00 16.41 D ATOM 6157 CZ PHE D 325 111.942 0.508 26.677 1.00 16.67 D ATOM 6158 C PHE D 325 115.640 5.798 28.136 1.00 21.95 D ATOM 6159 O PHE D 325 116.735 5.686 27.578 1.00 21.44 D ATOM 6160 N VAL D 326 115.240 6.925 28.707 1.00 21.18 D ATOM 6161 CA VAL D 326 116.059 8.113 28.642 1.00 21.85 D ATOM 6162 CB VAL D 326 115.922 8.765 27.238 1.00 21.90 D ATOM 6163 CG1 VAL D 326 114.455 9.085 26.972 1.00 22.16 D ATOM 6164 CG2 VAL D 326 116.772 10.016 27.133 1.00 19.90 D ATOM 6165 C VAL D 326 115.619 9.084 29.725 1.00 22.99 D ATOM 6166 O VAL D 326 114.453 9.105 30.121 1.00 23.26 D ATOM 6167 N SER D 327 116.571 9.869 30.215 1.00 26.57 D ATOM 6168 CA SER D 327 116.308 10.853 31.257 1.00 30.18 D ATOM 6169 CB SER D 327 117.552 11.111 32.099 1.00 28.88 D ATOM 6170 OG SER D 327 117.794 10.061 33.008 1.00 34.20 D ATOM 6171 C SER D 327 115.914 12.167 30.648 1.00 32.93 D ATOM 6172 O SER D 327 116.304 12.488 29.533 1.00 33.50 D ATOM 6173 N PRO D 328 115.141 12.958 31.384 1.00 36.30 D ATOM 6174 CD PRO D 328 114.483 12.591 32.644 1.00 38.28 D ATOM 6175 CA PRO D 328 114.693 14.269 30.923 1.00 38.59 D ATOM 6176 CB PRO D 328 113.988 14.834 32.140 1.00 38.19 D ATOM 6177 CG PRO D 328 113.360 13.609 32.728 1.00 39.16 D ATOM 6178 C PRO D 328 115.900 15.110 30.526 1.00 40.86 D ATOM 6179 O PRO D 328 115.886 15.787 29.496 1.00 42.18 D ATOM 6180 N LYS D 329 116.955 15.053 31.332 1.00 41.28 D ATOM 6181 CA LYS D 329 118.143 15.826 31.027 1.00 42.86 D ATOM 6182 CB LYS D 329 118.861 16.228 32.327 1.00 46.62 D ATOM 6183 CG LYS D 329 118.066 17.272 33.169 1.00 49.10 D ATOM 6184 CD LYS D 329 118.615 17.445 34.594 1.00 50.67 D ATOM 6185 CE LYS D 329 120.077 17.887 34.606 1.00 51.76 D ATOM 6186 NZ LYS D 329 120.645 17.988 35.993 1.00 51.50 D ATOM 6187 C LYS D 329 119.078 15.102 30.073 1.00 42.35 D ATOM 6188 O LYS D 329 120.060 15.671 29.609 1.00 43.19 D ATOM 6189 N GLY D 330 118.766 13.850 29.765 1.00 41.86 D ATOM 6190 CA GLY D 330 119.597 13.107 28.837 1.00 40.87 D ATOM 6191 C GLY D 330 118.961 13.089 27.456 1.00 42.32 D ATOM 6192 O GLY D 330 119.470 12.461 26.528 1.00 41.14 D ATOM 6193 N PHE D 331 117.849 13.798 27.304 1.00 44.29 D ATOM 6194 CA PHE D 331 117.148 13.809 26.026 1.00 46.40 D ATOM 6195 CB PHE D 331 115.887 14.660 26.119 1.00 47.33 D ATOM 6196 CG PHE D 331 114.896 14.396 25.016 1.00 49.12 D ATOM 6197 CD1 PHE D 331 114.198 13.188 24.958 1.00 48.42 D ATOM 6198 CD2 PHE D 331 114.658 15.359 24.033 1.00 49.78 D ATOM 6199 CE1 PHE D 331 113.273 12.942 23.939 1.00 48.28 D ATOM 6200 CE2 PHE D 331 113.735 15.128 23.008 1.00 49.07 D ATOM 6201 CZ PHE D 331 113.042 13.917 22.958 1.00 49.05 D ATOM 6202 C PHE D 331 117.983 14.276 24.846 1.00 46.95 D ATOM 6203 O PHE D 331 118.017 13.613 23.815 1.00 48.73 D ATOM 6204 N ASN D 332 118.651 15.414 24.997 1.00 47.11 D ATOM 6205 CA ASN D 332 119.477 15.972 23.932 1.00 46.02 D ATOM 6206 CB ASN D 332 120.255 17.161 24.463 1.00 47.82 D ATOM 6207 CG ASN D 332 119.497 18.440 24.335 1.00 49.50 D ATOM 6208 OD1 ASN D 332 118.322 18.519 24.692 1.00 50.47 D ATOM 6209 ND2 ASN D 332 120.165 19.468 23.815 1.00 52.34 D ATOM 6210 C ASN D 332 120.451 14.972 23.336 1.00 45.93 D ATOM 6211 O ASN D 332 120.420 14.681 22.140 1.00 45.54 D ATOM 6212 N SER D 333 121.326 14.443 24.175 1.00 46.43 D ATOM 6213 CA SER D 333 122.308 13.487 23.702 1.00 45.98 D ATOM 6214 CB SER D 333 123.043 12.863 24.885 1.00 46.48 D ATOM 6215 OG SER D 333 123.853 11.783 24.454 1.00 49.00 D ATOM 6216 C SER D 333 121.659 12.392 22.851 1.00 44.33 D ATOM 6217 O SER D 333 122.129 12.099 21.751 1.00 44.40 D ATOM 6218 N LED D 334 120.577 11.795 23.344 1.00 42.68 D ATOM 6219 CA LED D 334 119.912 10.728 22.591 1.00 41.52 D ATOM 6220 CB LED D 334 118.777 10.098 23.407 1.00 39.72 D ATOM 6221 CG LED D 334 117.873 9.152 22.604 1.00 38.51 D ATOM 6222 CD1 LED D 334 118.687 7.997 22.053 1.00 37.25 D ATOM 6223 CD2 LED D 334 116.746 8.651 23.475 1.00 37.57 D ATOM 6224 C LED D 334 119.352 11.228 21.268 1.00 39.88 D ATOM 6225 O LEU D 334 119.439 10.553 20.242 1.00 37.95 D ATOM 6226 N ASN D 335 118.758 12.410 21.304 1.00 39.39 D ATOM 6227 CA ASN D 335 118.202 12.973 20.096 1.00 39.71 D ATOM 6228 CB ASN D 335 117.463 14.263 20.399 1.00 40.92 D ATOM 6229 CG ASN D 335 116.080 14.255 19.829 1.00 42.75 D ATOM 6230 OD1 ASN D 335 115.879 13.877 18.676 1.00 43.99 D ATOM 6231 ND2 ASN D 335 115.108 14.669 20.630 1.00 44.96 D ATOM 6232 C ASN D 335 119.299 13.229 19.066 1.00 38.88 D ATOM 6233 O ASN D 335 119.209 12.772 17.926 1.00 39.28 D ATOM 6234 N LED D 336 120.341 13.945 19.469 1.00 36.54 D ATOM 6235 CA LED D 336 121.426 14.216 18.555 1.00 35.78 D ATOM 6236 CB LED D 336 122.488 15.081 19.230 1.00 35.28 D ATOM 6237 CG LED D 336 123.704 15.571 18.421 1.00 35.06 D ATOM 6238 CD1 LED D 336 124.755 14.482 18.364 1.00 33.88 D ATOM 6239 CD2 LED D 336 123.284 16.002 17.027 1.00 33.93 D ATOM 6240 C LED D 336 122.021 12.905 18.034 1.00 36.03 D ATOM 6241 O LED D 336 122.542 12.857 16.920 1.00 37.69 D ATOM 6242 N LYS D 337 121.919 11.833 18.812 1.00 36.19 D ATOM 6243 CA LYS D 337 122.439 10.529 18.378 1.00 37.20 D ATOM 6244 CB LYS D 337 122.452 9.533 19.547 1.00 38.40 D ATOM 6245 CG LYS D 337 123.706 9.512 20.409 1.00 40.10 D ATOM 6246 CD LYS D 337 124.743 8.543 19.848 1.00 41.01 D ATOM 6247 CE LYS D 337 125.896 8.283 20.827 1.00 41.41 D ATOM 6248 NZ LYS D 337 125.504 7.528 22.071 1.00 40.33 D ATOM 6249 C LYS D 337 121.576 9.939 17.257 1.00 37.31 D ATOM 6250 O LYS D 337 122.081 9.279 16.344 1.00 37.48 D ATOM 6251 N LED D 338 120.268 10.164 17.347 1.00 36.91 D ATOM 6252 CA LED D 338 119.332 9.654 16.351 1.00 36.87 D ATOM 6253 CB LED D 338 117.893 9.797 16.863 1.00 35.09 D ATOM 6254 CG LED D 338 117.529 8.902 18.052 1.00 33.33 D ATOM 6255 CD1 LED D 338 116.175 9.300 18.621 1.00 31.89 D ATOM 6256 CD2 LED D 338 117.533 7.450 17.600 1.00 31.70 D ATOM 6257 C LED D 338 119.513 10.412 15.044 1.00 37.22 D ATOM 6258 O LED D 338 119.418 9.841 13.968 1.00 36.68 D ATOM 6259 N SER D 339 119.791 11.703 15.161 1.00 37.23 D ATOM 6260 CA SER D 339 120.000 12.537 14.006 1.00 35.92 D ATOM 6261 CB SER D 339 120.390 13.933 14.426 1.00 34.24 D ATOM 6262 OG SER D 339 120.457 14.756 13.283 1.00 37.68 D ATOM 6263 C SER D 339 121.094 11.973 13.124 1.00 36.83 D ATOM 6264 O SER D 339 120.978 12.005 11.908 1.00 36.94 D ATOM 6265 N GLN D 340 122.161 11.467 13.735 1.00 36.98 D ATOM 6266 CA GLN D 340 123.266 10.895 12.975 1.00 37.54 D ATOM 6267 CB GLN D 340 124.443 10.581 13.883 1.00 38.76 D ATOM 6268 CG GLN D 340 124.489 11.408 15.144 1.00 42.76 D ATOM 6269 CD GLN D 340 125.519 12.491 15.095 1.00 43.21 D ATOM 6270 OE1 GLN D 340 125.816 13.113 16.105 1.00 43.96 D ATOM 6271 NE2 GLN D 340 126.077 12.727 13.917 1.00 47.75 D ATOM 6272 C GLN D 340 122.786 9.592 12.376 1.00 38.02 D ATOM 6273 O GLN D 340 123.099 9.254 11.235 1.00 36.84 D ATOM 6274 N LYS D 341 122.023 8.857 13.172 1.00 38.91 D ATOM 6275 CA LYS D 341 121.503 7.564 12.759 1.00 40.04 D ATOM 6276 CB LYS D 341 120.908 6.842 13.979 1.00 41.15 D ATOM 6277 CG LYS D 341 120.440 5.417 13.722 1.00 43.83 D ATOM 6278 CD LYS D 341 121.542 4.580 13.081 1.00 46.84 D ATOM 6279 CE LYS D 341 121.018 3.233 12.559 1.00 48.14 D ATOM 6280 NZ LYS D 341 122.101 2.428 11.901 1.00 48.02 D ATOM 6281 C LYS D 341 120.463 7.656 11.641 1.00 40.03 D ATOM 6282 O LYS D 341 120.548 6.935 10.647 1.00 40.71 D ATOM 6283 N TYR D 342 119.494 8.551 11.804 1.00 39.52 D ATOM 6284 CA TYR D 342 118.413 8.726 10.840 1.00 39.22 D ATOM 6285 CB TYR D 342 117.084 8.349 11.504 1.00 40.25 D ATOM 6286 CG TYR D 342 117.093 6.975 12.120 1.00 41.96 D ATOM 6287 CD1 TYR D 342 117.151 5.839 11.322 1.00 44.58 D ATOM 6288 CE1 TYR D 342 117.195 4.559 11.887 1.00 46.16 D ATOM 6289 CD2 TYR D 342 117.076 6.805 13.501 1.00 43.49 D ATOM 6290 CE2 TYR D 342 117.119 5.530 14.078 1.00 44.33 D ATOM 6291 CZ TYR D 342 117.180 4.412 13.263 1.00 45.41 D ATOM 6292 OH TYR D 342 117.244 3.145 13.796 1.00 44.64 D ATOM 6293 C TYR D 342 118.315 10.155 10.287 1.00 38.30 D ATOM 6294 O TYR D 342 117.437 10.926 10.687 1.00 38.68 D ATOM 6295 N PRO D 343 119.207 10.522 9.354 1.00 36.69 D ATOM 6296 CD PRO D 343 120.303 9.690 8.831 1.00 33.93 D ATOM 6297 CA PRO D 343 119.222 11.859 8.744 1.00 35.64 D ATOM 6298 CB PRO D 343 120.322 11.747 7.701 1.00 33.94 D ATOM 6299 CG PRO D 343 121.227 10.708 8.264 1.00 33.00 D ATOM 6300 C PRO D 343 117.897 12.243 8.100 1.00 36.66 D ATOM 6301 O PRO D 343 117.387 13.353 8.298 1.00 36.68 D ATOM 6302 N LYS D 344 117.345 11.306 7.333 1.00 37.98 D ATOM 6303 CA LYS D 344 116.097 11.521 6.600 1.00 38.87 D ATOM 6304 CB LYS D 344 116.021 10.554 5.402 1.00 40.52 D ATOM 6305 CG LYS D 344 116.552 9.140 5.658 1.00 43.94 D ATOM 6306 CD LYS D 344 115.598 8.274 6.494 1.00 44.39 D ATOM 6307 CE LYS D 344 116.370 7.166 7.227 1.00 43.37 D ATOM 6308 NZ LYS D 344 117.439 7.751 8.094 1.00 37.93 D ATOM 6309 C LYS D 344 114.791 11.471 7.396 1.00 37.24 D ATOM 6310 O LYS D 344 113.779 12.011 6.947 1.00 38.60 D ATOM 6311 N LEU D 345 114.808 10.851 8.572 1.00 34.93 D ATOM 6312 CA LEU D 345 113.597 10.766 9.382 1.00 32.64 D ATOM 6313 CB LEU D 345 113.670 9.573 10.329 1.00 31.24 D ATOM 6314 CG LEU D 345 113.726 8.216 9.628 1.00 29.39 D ATOM 6315 CD1 LEU D 345 113.660 7.118 10.667 1.00 30.86 D ATOM 6316 CD2 LEU D 345 112.560 8.084 8.666 1.00 30.92 D ATOM 6317 C LEU D 345 113.376 12.033 10.176 1.00 31.59 D ATOM 6318 O LEU D 345 114.318 12.780 10.422 1.00 32.92 D ATOM 6319 N SER D 346 112.130 12.298 10.557 1.00 30.59 D ATOM 6320 CA SER D 346 111.836 13.500 11.338 1.00 29.97 D ATOM 6321 CB SER D 346 110.377 13.931 11.158 1.00 29.48 D ATOM 6322 OG SER D 346 109.498 12.856 11.422 1.00 30.59 D ATOM 6323 C SER D 346 112.101 13.212 12.800 1.00 29.74 D ATOM 6324 O SER D 346 112.387 12.069 13.184 1.00 28.91 D ATOM 6325 N GLN D 347 111.992 14.233 13.634 1.00 28.38 D ATOM 6326 CA GLN D 347 112.255 13.991 15.036 1.00 28.40 D ATOM 6327 CB GLN D 347 112.237 15.291 15.818 1.00 29.66 D ATOM 6328 CG GLN D 347 112.819 15.144 17.190 1.00 32.02 D ATOM 6329 CD GLN D 347 112.905 16.474 17.879 1.00 35.29 D ATOM 6330 OE1 GLN D 347 111.889 17.161 18.035 1.00 38.15 D ATOM 6331 NE2 GLN D 347 114.111 16.861 18.292 1.00 33.64 D ATOM 6332 C GLN D 347 111.277 13.007 15.663 1.00 26.76 D ATOM 6333 O GLN D 347 111.694 12.085 16.357 1.00 26.57 D ATOM 6334 N GLN D 348 109.984 13.203 15.427 1.00 25.38 D ATOM 6335 CA GLN D 348 108.996 12.306 16.001 1.00 24.96 D ATOM 6336 CS GLN D 348 107.581 12.739 15.657 1.00 24.21 D ATOM 6337 CG GLN D 348 107.267 14.152 16.034 1.00 24.28 D ATOM 6338 CD GLN D 348 107.648 15.126 14.947 1.00 23.84 D ATOM 6339 OE1 GLN D 348 108.598 14.899 14.211 1.00 24.03 D ATOM 6340 NE2 GLN D 348 106.908 16.224 14.845 1.00 24.64 D ATOM 6341 C GLN D 348 109.209 10.896 15.483 1.00 26.54 D ATOM 6342 O GLN D 348 109.118 9.921 16.233 1.00 27.22 D ATOM 6343 N ASP D 349 109.499 10.791 14.193 1.00 26.70 D ATOM 6344 CA ASP D 349 109.718 9.500 13.588 1.00 26.16 D ATOM 6345 CB ASP D 349 109.918 9.666 12.086 1.00 30.05 D ATOM 6346 CG ASP D 349 108.666 9.338 11.295 1.00 33.76 D ATOM 6347 OD1 ASP D 349 107.598 9.889 11.612 1.00 35.36 D ATOM 6348 OD2 ASP D 349 108.754 8.521 10.354 1.00 37.16 D ATOM 6349 C ASP D 349 110.900 8.775 14.220 1.00 25.17 D ATOM 6350 O ASP D 349 110.815 7.578 14.508 1.00 25.67 D ATOM 6351 N ARG D 350 111.999 9.491 14.430 1.00 23.55 D ATOM 6352 CA ARG D 350 113.194 8.906 15.047 1.00 23.54 D ATOM 6353 CS ARG D 350 114.265 9.981 15.252 1.00 25.20 D ATOM 6354 CG ARG D 350 114.885 10.512 13.994 1.00 25.82 D ATOM 6355 CD ARG D 350 115.595 11.837 14.220 1.00 25.92 D ATOM 6356 NE ARG D 350 116.255 12.230 12.977 1.00 28.94 D ATOM 6357 CZ ARG D 350 116.707 13.448 12.698 1.00 29.47 D ATOM 6358 NH1 ARG D 350 116.590 14.440 13.568 1.00 32.83 D ATOM 6359 NH2 ARG D 350 117.281 13.673 11.534 1.00 31.17 D ATOM 6360 C ARG D 350 112.831 8.343 16.416 1.00 23.18 D ATOM 6361 O ARG D 350 112.968 7.148 16.679 1.00 22.24 D ATOM 6362 N LEU D 351 112.376 9.242 17.282 1.00 21.94 D ATOM 6363 CA LEU D 351 111.991 8.890 18.627 1.00 20.55 D ATOM 6364 CB LEU D 351 111.307 10.082 19.297 1.00 18.30 D ATOM 6365 CG LEU D 351 112.227 11.278 19.543 1.00 15.70 D ATOM 6366 CD1 LEU D 351 111.401 12.443 19.998 1.00 14.97 D ATOM 6367 CD2 LEU D 351 113.315 10.927 20.561 1.00 12.36 D ATOM 6368 C LEU D 351 111.081 7.671 18.627 1.00 20.79 D ATOM 6369 O LEU D 351 111.175 6.824 19.508 1.00 21.85 D ATOM 6370 N ARG D 352 110.211 7.569 17.631 1.00 21.27 D ATOM 6371 CA ARG D 352 109.333 6.421 17.566 1.00 22.32 D ATOM 6372 CB ARG D 352 108.251 6.616 16.517 1.00 23.50 D ATOM 6373 CG ARG D 352 107.278 5.440 16.398 1.00 25.41 D ATOM 6374 CD ARG D 352 106.075 5.874 15.568 1.00 26.94 D ATOM 6375 NE ARG D 352 106.491 6.312 14.248 1.00 27.67 D ATOM 6376 CZ ARG D 352 106.345 5.590 13.151 1.00 27.98 D ATOM 6377 NH1 ARG D 352 105.772 4.384 13.223 1.00 28.77 D ATOM 6378 NH2 ARG D 352 106.801 6.071 11.997 1.00 28.35 D ATOM 6379 C ARG D 352 110.132 5.156 17.257 1.00 22.65 D ATOM 6380 O ARG D 352 109.852 4.088 17.809 1.00 22.75 D ATOM 6381 N LEU D 353 111.129 5.236 16.389 1.00 23.22 D ATOM 6382 CA LEU D 353 111.877 4.014 16.139 1.00 25.64 D ATOM 6383 CB LEUD D 353 112.853 4.180 14.974 1.00 27.60 D ATOM 6384 CG LEU D 353 112.211 4.675 13.687 1.00 31.53 D ATOM 6385 CD1 LEU D 353 113.257 4.543 12.590 1.00 34.73 D ATOM 6386 CD2 LEU D 353 110.948 3.847 13.321 1.00 34.02 D ATOM 6387 C LEU D 353 112.640 3.650 17.408 1.00 24.34 D ATOM 6388 O LEU D 353 112.766 2.477 17.748 1.00 24.26 D ATOM 6389 N SER D 354 113.135 4.654 18.124 1.00 24.48 D ATOM 6390 CA SER D 354 113.888 4.379 19.339 1.00 24.64 D ATOM 6391 CB SER D 354 114.399 5.670 19.953 1.00 24.29 O ATOM 6392 OG SER D 354 115.774 5.509 20.223 1.00 27.22 O ATOM 6393 C SER D 354 113.045 3.623 20.345 1.00 23.77 D ATOM 6394 O SER D 354 113.439 2.566 20.828 1.00 22.40 D ATOM 6395 N PHE D 355 111.879 4.169 20.646 1.00 23.57 D ATOM 6396 CA PHE D 355 110.979 3.533 21.573 1.00 25.63 D ATOM 6397 CB PHE D 355 109.660 4.283 21.596 1.00 26.61 D ATOM 6398 CG PHE D 355 108.725 3.795 22.636 1.00 27.78 D ATOM 6399 CD1 PHE D 355 109.055 3.919 23.978 1.00 29.88 D ATOM 6400 CD2 PHE D 355 107.526 3.189 22.286 1.00 29.67 D ATOM 6401 CE1 PHE D 355 108.205 3.443 24.972 1.00 29.34 D ATOM 6402 CE2 PHE D 355 106.664 2.707 23.269 1.00 30.25 D ATOM 6403 CZ PHE D 355 107.011 2.836 24.614 1.00 29.64 D ATOM 6404 C PHE D 355 110.731 2.089 21.156 1.00 26.53 D ATOM 6405 O PHE D 355 110.970 1.156 21.920 1.00 26.93 D ATOM 6406 N LEU D 356 110.257 1.904 19.931 1.00 27.97 D ATOM 6407 CA LEU D 356 109.975 0.557 19.441 1.00 29.40 D ATOM 6408 CB LEU D 356 109.502 0.601 17.990 1.00 29.41 D ATOM 6409 CG LEU D 356 108.233 1.408 17.701 1.00 30.81 D ATOM 6410 CD1 LEU D 356 108.091 1.510 16.193 1.00 30.03 D ATOM 6411 CD2 LEU D 356 107.001 0.766 18.334 1.00 27.79 D ATOM 6412 C LEU D 35 111.164 −0.387 19.557 1.00 29.19 D ATOM 6413 O LEU D 356 111.011 −1.540 19.954 1.00 29.03 D ATOM 6414 N GLU D 357 112.348 0.106 19.223 1.00 29.15 D ATOM 6415 CA GLU D 357 113.525 −0.723 19.296 1.00 30.63 D ATOM 6416 CB GLU D 357 114.677 −0.053 18.560 1.00 32.16 D ATOM 6417 CG GLU D 357 115.697 −1.025 18.007 1.00 37.30 D ATOM 6418 CD GLU D 357 117.086 −0.418 17.930 1.00 40.82 D ATOM 6419 OE1 GLU D 357 117.248 0.639 17.262 1.00 41.37 D ATOM 6420 OE2 GLU D 357 118.017 −1.000 18.548 1.00 41.48 D ATOM 6421 C GLU D 357 113.946 −1.025 20.741 1.00 32.26 D ATOM 6422 O GLU D 357 114.599 −2.041 21.016 1.00 31.90 D ATOM 6423 N ASN D 358 113.571 −0.148 21.665 1.00 29.36 D ATOM 6424 CA ASN D 358 113.939 −0.341 23.046 1.00 27.42 D ATOM 6425 CB ASN D 358 114.060 1.000 23.750 1.00 27.90 D ATOM 6426 CG ASN D 358 115.443 1.598 23.610 1.00 28.81 D ATOM 6427 OD1 ASN D 358 115.621 2.656 23.006 1.00 29.58 D ATOM 6428 ND2 ASN D 358 116.439 0.916 24.171 1.00 29.80 D ATOM 6429 C ASN D 358 112.996 −1.248 23.793 1.00 27.49 D ATOM 6430 O ASN D 358 113.404 −1.974 24.700 1.00 27.75 D ATOM 6431 N ILE D 359 111.732 −1.217 23.408 1.00 27.57 D ATOM 6432 CA ILE D 359 110.757 −2.076 24.046 1.00 28.89 D ATOM 6433 CB ILE D 359 109.361 −1.821 23.510 1.00 29.72 D ATOM 6434 CG2 ILE D 359 108.342 −2.575 24.322 1.00 28.76 D ATOM 6435 OG1 ILE D 359 109.058 −0.336 23.581 1.00 32.82 D ATOM 6436 CD1 ILE D 359 108.196 0.120 22.444 1.00 36.53 D ATOM 6437 C ILE D 359 111.161 −3.466 23.629 1.00 28.09 D ATOM 6438 O ILE D 359 111.164 −4.389 24.425 1.00 27.60 D ATOM 6439 N PHE D 360 111.518 −3.592 22.361 1.00 29.39 D ATOM 6440 CA PHE D 360 111.926 −4.864 21.810 1.00 30.15 D ATOM 6441 CB PHE D 360 112.415 −4.654 20.372 1.00 32.47 D ATOM 6442 CG PHE D 360 112.998 −5.885 19.738 1.00 33.66 D ATOM 6443 CD1 PHE D 360 112.236 −7.045 19.600 1.00 34.21 D ATOM 6444 CD2 PHE D 360 114.327 −5.898 19.326 1.00 34.66 D ATOM 6445 CE1 PHE D 360 112.790 −8.201 19.071 1.00 34.86 D ATOM 6446 CE2 PHE D 360 114.894 −7.044 18.796 1.00 36.23 D ATOM 6447 CZ PHE D 360 114.124 −8.202 18.670 1.00 35.77 D ATOM 6448 C PHE D 360 113.015 −5.503 22.654 1.00 29.32 D ATOM 6449 O PHE D 360 112.879 −6.641 23.092 1.00 29.82 D ATOM 6450 N ILE D 361 114.093 −4.762 22.880 1.00 28.24 D ATOM 6451 CA ILE D 361 115.222 −5.254 23.660 1.00 26.57 D ATOM 6452 CB ILE D 361 116.376 −4.219 23.597 1.00 26.56 D ATOM 6453 CG2 ILE D 361 117.540 −4.638 24.502 1.00 24.26 D ATOM 6454 CG1 ILE D 361 116.855 −4.117 22.140 1.00 25.22 D ATOM 6455 CD1 ILE D 361 117.841 −3.000 21.868 1.00 25.88 D ATOM 6456 C ILE D 361 114.834 −5.578 25.111 1.00 25.14 D ATOM 6457 O ILE D 361 115.238 −6.610 25.656 1.00 24.17 D ATOM 6458 N LEU D 362 114.027 −4.712 25.718 1.00 22.80 D ATOM 6459 CA LEU D 362 113.591 −4.915 27.098 1.00 23.19 D ATOM 6460 CB LEU D 362 112.801 −3.700 27.576 1.00 20.92 D ATOM 6461 CG LEU D 362 112.565 −3.604 29.077 1.00 20.66 D ATOM 6462 CD1 LEU D 362 113.860 −3.753 29.867 1.00 18.78 D ATOM 6463 CD2 LEU D 362 111.917 −2.273 29.338 1.00 20.71 D ATOM 6464 C LEU D 362 112.773 −6.196 27.330 1.00 23.63 D ATOM 6465 O LEU D 362 112.997 −6.915 28.311 1.00 23.67 D ATOM 6466 N LYS D 363 111.824 −6.453 26.434 1.00 23.53 D ATOM 6467 CA LYS D 363 110.986 −7.639 26.477 1.00 24.42 D ATOM 6468 CB LYS D 363 110.156 −7.743 25.191 1.00 26.43 D ATOM 6469 CG LYS D 363 108.730 −7.209 25.270 1.00 30.86 D ATOM 6470 CD LYS D 363 108.669 −5.840 25.929 1.00 33.41 D ATOM 6471 CE LYS D 363 107.226 −5.421 26.252 1.00 35.72 D ATOM 6472 NZ LYS D 363 107.204 −4.294 27.264 1.00 35.50 D ATOM 6473 C LYS D 363 111.901 −8.859 26.573 1.00 25.36 D ATOM 6474 O LYS D 363 111.629 −9.802 27.311 1.00 25.60 D ATOM 6475 N ASN D 364 112.988 −8.829 25.809 1.00 25.23 D ATOM 6476 CA ASN D 364 113.935 −9.927 25.799 1.00 25.39 D ATOM 6477 CB ASN D 364 114.980 −9.737 24.712 1.00 25.02 D ATOM 6478 CG ASN D 364 114.436 −9.985 23.348 1.00 26.12 D ATOM 6479 OD1 ASN D 364 115.038 −9.589 22.348 1.00 25.32 D ATOM 6480 ND2 ASN D 364 113.286 −10.66 223.283 1.00 27.95 D ATOM 6481 C ASN D 364 114.640 −10.030 27.118 1.00 26.63 D ATOM 6482 O ASN D 364 114.785 −11.120 27.665 1.00 28.76 D ATOM 6483 N TRP D 365 115.101 −8.901 27.635 1.00 26.04 D ATOM 6484 CA TRP D 365 115.794 −8.937 28.906 1.00 25.62 D ATOM 6485 CB TRP D 365 116.211 −7.535 29.357 1.00 23.36 D ATOM 6486 CG TRP D 365 117.514 −7.035 28.789 1.00 19.48 D ATOM 6487 CD2 TRP D 365 118.801 −7.069 29.427 1.00 16.99 D ATOM 6488 CE2 TRP D 365 119.706 −6.410 28.572 1.00 15.60 D ATOM 6489 CE3 TRP D 365 119.275 −7.589 30.640 1.00 15.17 D ATOM 6490 CD1 TRP D 365 117.691 −6.387 27.613 1.00 17.39 D ATOM 6491 NE1 TRP D 365 119.001 −6.003 27.473 1.00 14.98 D ATOM 6492 CZ2 TRP D 365 121.072 −6.249 28.892 1.00 15.36 D ATOM 6493 CZ3 TRP D 365 120.628 −7.428 30.956 1.00 13.84 D ATOM 6494 CH2 TRP D 365 121.509 −6.762 30.081 1.00 10.82 D ATOM 6495 C TRP D 365 114.868 −9.538 29.947 1.00 26.26 D ATOM 6496 O TRP D 365 115.267 −10.422 30.693 1.00 28.48 D ATOM 6497 N TYR D 366 113.621 −9.084 29.956 1.00 24.80 D ATOM 6498 CA TYR D 366 112.641 −9.530 30.934 1.00 23.32 D ATOM 6499 CB TYR D 366 111.480 −8.553 30.947 1.00 17.63 D ATOM 6500 CG TYR D 366 111.793 −7.211 31.597 1.00 16.02 D ATOM 6501 CD1 TYR D 366 113.058 −6.914 32.118 1.00 14.32 D ATOM 6502 CE1 TYR D 366 113.304 −5.681 32.726 1.00 11.48 D ATOM 6503 CD2 TYR D 366 110.808 −6.243 31.712 1.00 13.79 D ATOM 6504 CE2 TYR D 366 111.054 −5.033 32.320 1.00 11.61 D ATOM 6505 CZ TYR D 366 112.283 −4.760 32.812 1.00 11.97 D ATOM 6506 OH TYR D 366 112.475 −3.532 33.364 1.00 15.79 D ATOM 6507 C TYR D 366 112.112 −10.939 30.762 1.00 25.30 D ATOM 6508 O TYR D 366 111.620 −11.548 31.715 1.00 25.60 D ATOM 6509 N ASN D 367 112.227 −11.441 29.538 1.00 27.79 D ATOM 6510 CA ASN D 367 111.757 −12.770 29.160 1.00 28.52 D ATOM 6511 CE ASN D 367 111.596 −12.837 27.642 1.00 29.23 D ATOM 6512 CG ASN D 367 111.047 −14.162 27.168 1.00 29.51 D ATOM 6513 OD1 ASN D 367 111.045 −15.165 27.907 1.00 29.16 D ATOM 6514 ND2 ASN D 367 110.588 −14.183 25.915 1.00 28.51 D ATOM 6515 C ASN D 367 112.706 −13.872 29.617 1.00 28.04 D ATOM 6516 O ASN D 367 113.779 −14.076 29.042 1.00 28.99 D ATOM 6517 N PRO D 368 112.306 −14.606 30.659 1.00 27.46 D ATOM 6518 CD PRO D 368 111.038 −14.427 31.394 1.00 27.49 D ATOM 6519 CA PRO D 368 113.094 −15.701 31.228 1.00 26.35 D ATOM 6520 CB PRO D 368 112.174 −16.249 32.313 1.00 26.40 D ATOM 6521 CG PRO D 368 111.350 −15.041 32.703 1.00 26.24 D ATOM 6522 C PRO D 368 113.470 −16.766 30.207 1.00 25.90 D ATOM 6523 O PRO D 368 114.556 −17.338 30.270 1.00 23.69 D ATOM 6524 N LYS D 369 112.570 −17.027 29.264 1.00 26.98 D ATOM 6525 CA LYS D 369 112.815 −18.051 28.249 1.00 27.69 D ATOM 6526 CB LYS D 369 111.483 −18.478 27.605 1.00 27.37 D ATOM 6527 CG LYS D 369 111.523 −19.857 26.933 1.00 28.34 D ATOM 6528 CD LYS D 369 110.159 −20.280 26.431 0.00 28.71 D ATOM 6529 CE LYS D 369 109.692 −19.395 25.288 0.00 29.07 D ATOM 6530 NZ LYS D 369 108.385 −19.851 24.737 0.00 29.21 D ATOM 6531 C LYS D 369 113.815 −17.602 27.170 1.00 28.21 D ATOM 6532 O LYS D 369 114.404 −18.432 26.466 1.00 27.80 D ATOM 6533 N PHE D 370 114.027 −16.295 27.055 1.00 28.20 D ATOM 6534 CA PHE D 370 114.945 −15.779 26.048 1.00 29.53 D ATOM 6535 CB PHE D 370 114.804 −14.267 25.930 1.00 30.24 D ATOM 6536 CG PHE D 370 115.741 −13.647 24.926 1.00 31.46 D ATOM 6537 CD1 PHE D 370 117.107 −13.497 25.208 1.00 32.17 D ATOM 6538 CD2 PHE D 370 115.253 −13.184 23.711 1.00 31.98 D ATOM 6539 CE1 PHE D 370 117.970 −12.894 24.301 1.00 30.34 D ATOM 6540 CE2 PHE D 370 116.105 −12.580 22.795 1.00 32.40 D ATOM 6541 CZ PHE D 370 117.473 −12.434 23.098 1.00 31.69 D ATOM 6542 C PHE D 370 116.418 −16.125 26.250 1.00 29.47 D ATOM 6543 O PHE D 370 116.990 −15.909 27.323 1.00 30.76 D ATOM 6544 N VAL D 371 117.038 −16.623 25.186 1.00 28.02 D ATOM 6545 CA VAL D 371 118.441 −16.986 25.252 1.00 27.30 D ATOM 6546 CB VAL D 371 118.648 −18.446 24.756 1.00 26.04 D ATOM 6547 CG1 VAL D 371 120.104 −18.829 24.825 1.00 22.81 D ATOM 6548 CG2 VAL D 371 117.827 −19.396 25.624 1.00 22.71 D ATOM 6549 C VAL D 371 119.309 −15.995 24.469 1.00 28.27 D ATOM 6550 O VAL D 371 119.221 −15.880 23.248 1.00 27.93 D ATOM 6551 N PRO D 372 120.161 −15.251 25.188 1.00 29.70 D ATOM 6552 CD PRO D 372 120.326 −15.276 26.648 1.00 29.18 D ATOM 6553 CA PRO D 372 121.057 −14.258 24.597 1.00 31.17 D ATOM 6554 CB PRO D 372 121.744 −13.642 25.816 1.00 29.97 D ATOM 6555 CG PRO D 372 120.796 −13.886 26.914 1.00 30.31 D ATOM 6556 C PRO D 372 122.071 −14.884 23.659 1.00 32.23 D ATOM 6557 O PRO D 372 122.136 −16.104 23.515 1.00 33.92 D ATOM 6558 N GLN D 373 122.860 −14.033 23.019 1.00 32.64 D ATOM 6559 CA GLN D 373 123.907 −14.511 22.144 1.00 31.91 D ATOM 6560 CB GLN D 373 123.945 −13.701 20.865 1.00 31.03 D ATOM 6561 CG GLN D 373 124.881 −14.279 19.845 1.00 31.69 D ATOM 6562 CD GLN D 373 125.575 −13.202 19.069 1.00 32.49 D ATOM 6563 OE1 GLN D 373 124.937 −12.328 18.502 1.00 33.06 D ATOM 6564 NE2 GLN D 373 126.892 −13.251 19.045 1.00 34.46 D ATOM 6565 C GLN D 373 125.203 −14.315 22.925 1.00 31.35 D ATOM 6566 O GLN D 373 125.612 −13.192 23.224 1.00 31.52 D ATOM 6567 N ARG D 374 125.842 −15.418 23.264 1.00 29.71 D ATOM 6568 CA ARG D 374 127.059 −15.342 24.024 1.00 29.87 D ATOM 6569 CB ARG D 374 127.054 −16.417 25.102 1.00 30.39 D ATOM 6570 CG ARG D 374 128.347 −16.511 25.854 1.00 31.03 D ATOM 6571 CD ARG D 374 128.261 −17.597 26.873 1.00 31.27 D ATOM 6572 NE ARG D 374 129.475 −17.599 27.658 1.00 32.88 D ATOM 6573 CZ ARG D 374 129.738 −18.450 28.637 1.00 33.11 D ATOM 6574 NH1 ARG D 374 128.856 −19.390 28.956 1.00 31.68 D ATOM 6575 NH2 ARG D 374 130.889 −18.343 29.301 1.00 33.83 D ATOM 6576 C ARG D 374 128.306 −15.477 23.161 1.00 30.20 D ATOM 6577 O ARG D 374 128.383 −16.319 22.268 1.00 30.52 D ATOM 6578 N THR D 375 129.298 −14.654 23.463 1.00 30.06 D ATOM 6579 CA THR D 375 130.543 −14.641 22.724 1.00 29.07 D ATOM 6580 CB THR D 375 130.574 −13.423 21.801 1.00 29.18 D ATOM 6581 OG1 THR D 375 129.254 −13.177 21.294 1.00 30.22 D ATOM 6582 CG2 THR D 375 131.520 −13.650 20.650 1.00 27.55 D ATOM 6583 C THR D 375 131.666 −14.506 23.749 1.00 29.99 D ATOM 6584 O THR D 375 131.743 −13.505 24.473 1.00 30.81 D ATOM 6585 N THR D 376 132.537 −15.504 23.824 1.00 29.02 D ATOM 6586 CA THR D 376 133.631 −15.459 24.789 1.00 28.35 D ATOM 6587 CB THR D 376 133.775 −16.810 25.551 1.00 26.89 D ATOM 6588 OG1 THR D 376 132.516 −17.174 26.129 1.00 24.67 D ATOM 6589 CG2 THR D 376 134.822 −16.700 26.648 1.00 25.06 D ATOM 6590 C THR D 376 134.959 −15.155 24.120 1.00 29.32 D ATOM 6591 O THR D 376 135.386 −15.886 23.234 1.00 28.86 D ATOM 6592 N LEU D 377 135.616 −14.081 24.555 1.00 31.19 D ATOM 6593 CA LEU D 377 136.916 −13.701 24.001 1.00 33.04 D ATOM 6594 CS LEU D 377 136.888 −12.242 23.558 1.00 31.62 D ATOM 6595 CG LEU D 377 135.621 −11.843 22.793 1.00 32.74 D ATOM 6596 CD1 LEU D 377 135.718 −10.396 22.376 1.00 32.01 D ATOM 6597 CD2 LEU D 377 135.430 −12.735 21.590 1.00 32.02 D ATOM 6598 C LEU D 377 138.006 −13.907 25.044 1.00 35.05 D ATOM 6599 O LEU D 377 137.733 −13.877 26.241 1.00 36.55 D ATOM 6600 N ARG D 378 139.238 −14.122 24.590 1.00 37.30 D ATOM 6601 CA ARG D 378 140.381 −14.341 25.487 1.00 38.75 D ATOM 6602 CS ARG D 378 141.620 −14.732 24.661 1.00 41.44 D ATOM 6603 CG ARG D 378 142.735 −15.467 25.412 1.00 45.29 D ATOM 6604 CD ARG D 378 143.962 −15.705 24.499 1.00 49.27 D ATOM 6605 NE ARG D 378 144.615 −14.445 24.116 1.00 53.86 D ATOM 6606 CZ ARG D 378 145.636 −14.322 23.260 1.00 55.92 D ATOM 6607 NH1 ARG D 378 146.147 −15.400 22.666 1.00 55.78 D ATOM 6608 NH2 ARG D 378 146.152 −13.109 23.009 1.00 55.08 D ATOM 6609 C ARG D 378 140.663 −13.056 26.259 1.00 38.43 D ATOM 6610 O ARG D 378 140.498 −11.956 25.723 1.00 37.88 D ATOM 6611 N GLY D 379 141.098 −13.206 27.510 1.00 38.54 D ATOM 6612 CA GLY D 379 141.408 −12.058 28.349 1.00 38.37 D ATOM 6613 C GLY D 379 142.901 −11.817 28.563 1.00 38.46 D ATOM 6614 O GLY D 379 143.704 −12.014 27.646 1.00 39.93 D ATOM 6615 N HIS D380 143.270 −11.390 29.771 1.00 36.54 D ATOM 6616 CA HIS D 380 144.663 −11.116 30.118 1.00 35.40 D ATOM 6617 CB HIS D 380 144.735 −10.098 31.259 1.00 32.54 D ATOM 6618 CG HIS D 380 144.169 −8.762 30.910 1.00 29.64 D ATOM 6619 CD2 HIS D 380 144.748 −7.541 30.837 1.00 29.11 D ATOM 6620 ND1 HIS D 380 142.845 −8.580 30.581 1.00 28.66 D ATOM 6621 CE1 HIS D 380 142.630 −7.302 30.323 1.00 26.84 D ATOM 6622 NE2 HIS D 380 143.768 −6.650 30.470 1.00 28.50 D ATOM 6623 C HIS D 380 145.400 −12.389 30.524 1.00 35.86 D ATOM 6624 O HIS D 380 144.796 −13.450 30.606 1.00 35.08 D ATOM 6625 N MSE D 381 146.699 −12.287 30.790 1.00 37.57 D ATOM 6626 CA MSE D 381 147.467 −13.465 31.172 1.00 40.68 D ATOM 6627 CS MSE D 381 148.937 −13.253 30.850 1.00 42.82 D ATOM 6628 CG MSE D 381 149.177 −13.111 29.372 1.00 45.44 D ATOM 6629 SE MSE D 381 150.909 −12.445 28.929 1.00 55.08 D ATOM 6630 CE MSE D 381 150.582 −10.533 29.001 1.00 48.67 D ATOM 6631 C MSE D 381 147.306 −13.812 32.645 1.00 41.59 D ATOM 6632 O MSE D 381 147.979 −14.701 33.169 1.00 40.94 D ATOM 6633 N THR D 382 146.392 −13.103 33.296 1.00 42.55 D ATOM 6634 CA THR D 382 146.091 −13.286 34.704 1.00 42.91 D ATOM 6635 CB THR D 382 146.571 −12.035 35.487 1.00 42.87 D ATOM 6636 OG1 THR D 382 146.096 −12.083 36.838 1.00 47.41 D ATOM 6637 CG2 THR D 382 146.091 −10.770 34.806 1.00 42.47 D ATOM 6638 C THR D 382 144.566 −13.490 34.809 1.00 42.80 D ATOM 6639 O THR D 382 143.799 −12.695 34.280 1.00 45.02 D ATOM 6640 N SER D 383 144.129 −14.559 35.466 1.00 41.05 D ATOM 6641 CA SER D 383 142.708 −14.855 35.590 1.00 40.03 D ATOM 6642 CB SER D 383 142.527 −16.201 36.285 1.00 41.63 D ATOM 6643 OG SER D 383 143.273 −16.252 37.491 1.00 42.67 D ATOM 6644 C SER D 383 141.888 −13.806 36.323 1.00 38.85 D ATOM 6645 O SER D 383 140.701 −14.007 36.569 1.00 39.35 D ATOM 6646 N VAL D 384 142.514 −12.689 36.665 1.00 37.95 D ATOM 6647 CA VAL D 384 141.829 −11.620 37.382 1.00 37.40 D ATOM 6648 CB VAL D 384 142.471 −11.414 38.777 1.00 39.34 D ATOM 6649 CG1 VAL D 384 141.606 −10.515 39.638 1.00 39.21 D ATOM 6650 CG2 VAL D 384 142.672 −12.756 39.451 1.00 41.87 D ATOM 6651 C VAL D 384 141.899 −10.302 36.615 1.00 35.77 D ATOM 6652 O VAL D 384 142.987 −9.824 36.282 1.00 35.80 D ATOM 6653 N ILE D 385 140.741 −9.719 36.330 1.00 33.56 D ATOM 6654 CA ILE D 385 140.697 −8.445 35.627 1.00 31.75 D ATOM 6655 CB ILE D 385 139.503 −8.347 34.670 1.00 32.21 D ATOM 6656 CG2 ILE D 385 139.566 −7.028 33.924 1.00 31.42 D ATOM 6657 CG1 ILE D 385 139.528 −9.506 33.673 1.00 34.12 D ATOM 6658 CD1 ILE D 385 140.728 −9.519 32.787 1.00 31.79 D ATOM 6659 C ILE D 385 140.524 −7.369 36.681 1.00 29.87 D ATOM 6660 O ILE D 385 139.636 −7.468 37.523 1.00 29.33 D ATOM 6661 N THR D 386 141.364 −6.341 36.631 1.00 28.00 D ATOM 6662 CA THR D 386 141.284 −5.262 37.603 1.00 26.59 D ATOM 6663 CB THR D 386 142.665 −4.709 37.933 1.00 28.33 D ATOM 6664 OG1 THR D 386 143.147 −3.965 36.810 1.00 33.14 D ATOM 6665 CG2 THR D 386 143.629 −5.847 38.258 1.00 27.95 D ATOM 6666 C THR D 386 140.370 −4.095 37.219 1.00 23.96 D ATOM 6667 O THR D 386 140.049 −3.258 38.057 1.00 23.82 D ATOM 6668 N CYS D 387 139.969 −4.000 35.959 1.00 21.99 D ATOM 6669 CA CYS D 387 139.032 −2.946 35.583 1.00 21.32 D ATOM 6670 CB CYS D 387 139.593 −1.554 35.810 1.00 21.52 D ATOM 6671 SG CYS D 387 141.286 −1.370 35.494 1.00 24.48 D ATOM 6672 C CYS D 387 138.522 −3.058 34.185 1.00 20.32 D ATOM 6673 O CYS D 387 139.180 −3.609 33.309 1.00 20.62 D ATOM 6674 N LEU D 388 137.313 −2.554 33.993 1.00 21.13 D ATOM 6675 CA LEU D 388 136.666 −2.620 32.699 1.00 21.99 D ATOM 6676 CB LEU D 388 135.720 −3.811 32.699 1.00 19.44 D ATOM 6677 CG LEU D 388 134.666 −3.896 31.603 1.00 17.83 D ATOM 6678 CD1 LEU D 388 134.369 −5.364 31.382 1.00 19.58 D ATOM 6679 CD2 LEU D 388 133.406 −3.172 32.009 1.00 17.27 D ATOM 6680 C LEU D 388 135.910 −1.349 32.307 1.00 23.54 D ATOM 6681 O LEU D 388 135.262 −0.724 33.136 1.00 24.86 D ATOM 6682 N GLN D 389 136.011 −0.965 31.038 1.00 25.33 D ATOM 6683 CA GLN D 389 135.302 0.203 30.521 1.00 25.28 D ATOM 6684 CB GLN D 389 136.275 1.296 30.073 1.00 25.97 D ATOM 6685 CG GLN D 389 137.029 2.071 31.150 1.00 25.10 D ATOM 6686 CD GLN D 389 136.179 3.114 31.877 1.00 26.41 D ATOM 6687 OE1 GLN D 389 135.673 2.850 32.949 1.00 26.25 D ATOM 6688 NE2 GLN D 389 136.031 4.304 31.293 1.00 27.94 D ATOM 6689 C GLN D 389 134.477 −0.233 29.303 1.00 26.25 D ATOM 6690 O GLN D 389 134.917 −1.076 28.515 1.00 26.39 D ATOM 6691 N PHE D 390 133.284 0.340 29.153 1.00 27.94 D ATOM 6692 CA PHE D 390 132.415 0.045 28.015 1.00 28.91 D ATOM 6693 CB PHE D 390 131.364 −0.995 28.424 1.00 26.05 D ATOM 6694 CG PHE D 390 130.416 −1.381 27.322 1.00 26.58 D ATOM 6695 CD1 PHE D 390 130.826 −1.411 25.998 1.00 27.31 D ATOM 6696 CD2 PHE D 390 129.087 −1.675 27.609 1.00 27.25 D ATOM 6697 CE1 PHE D 390 129.921 −1.716 24.978 1.00 26.45 D ATOM 6698 CE2 PHE D 390 128.179 −1.982 26.595 1.00 26.66 D ATOM 6699 CZ PHE D 390 128.597 −1.999 25.284 1.00 25.88 D ATOM 6700 C PHE D 390 131.800 1.375 27.521 1.00 31.17 D ATOM 6701 O PHE D 390 130.844 1.911 28.095 1.00 31.73 D ATOM 6702 N GLU D 391 132.404 1.908 26.460 1.00 33.23 D ATOM 6703 CA GLU D 391 132.004 3.172 25.842 1.00 36.52 D ATOM 6704 CB GLU D 391 132.752 4.335 26.494 1.00 37.25 D ATOM 6705 CG GLU D 391 131.870 5.425 27.041 1.00 38.77 D ATOM 6706 CD GLU D 391 131.258 5.032 28.354 1.00 39.09 D ATOM 6707 OE1 GLU D 391 132.023 4.888 29.322 1.00 40.49 D ATOM 6708 OE2 GLU D 391 130.024 4.859 28.417 1.00 39.48 D ATOM 6709 C GLU D 391 132.377 3.150 24.360 1.00 37.92 D ATOM 6710 O GLU D 391 133.293 2.426 23.956 1.00 39.21 D ATOM 6711 N ASP D 392 131.704 3.971 23.557 1.00 38.58 D ATOM 6712 CA ASP D 392 131.986 4.053 22.112 1.00 38.07 D ATOM 6713 CB ASP D 392 133.157 5.009 21.858 1.00 37.43 D ATOM 6714 CG ASP D 392 132.716 6.428 21.778 1.00 39.32 D ATOM 6715 OD1 ASP D 392 131.501 6.650 21.954 1.00 40.76 D ATOM 6716 OD2 ASP D 392 133.557 7.317 21.530 1.00 40.53 D ATOM 6717 C ASP D 392 132.253 2.725 21.400 1.00 36.82 D ATOM 6718 O ASP D 392 133.221 2.589 20.647 1.00 36.96 D ATOM 6719 N ASN D 393 131.381 1.753 21.631 1.00 35.81 D ATOM 6720 CA ASN D 393 131.513 0.448 21.000 1.00 36.51 D ATOM 6721 CB ASN D 393 131.410 0.572 19.471 1.00 37.62 D ATOM 6722 CG ASN D 393 130.111 1.264 19.001 1.00 39.78 D ATOM 6723 OD1 ASN D 393 130.023 1.696 17.846 1.00 41.53 D ATOM 6724 ND2 ASN D 393 129.111 1.362 19.881 1.00 38.28 D ATOM 6725 C ASN D 393 132.829 −0.215 21.366 1.00 34.65 D ATOM 6726 O ASN D 393 133.249 −1.163 20.710 1.00 34.87 D ATOM 6727 N TYR D 394 133.477 0.292 22.409 1.00 33.42 D ATOM 6728 CA TYR D 394 134.742 −0.264 22.884 1.00 32.37 D ATOM 6729 CB TYR D 394 135.783 0.838 23.102 1.00 32.07 D ATOM 6730 CG TYR D 394 136.458 1.349 21.860 1.00 32.95 D ATOM 6731 CD1 TYR D 394 137.124 0.479 20.992 1.00 32.58 D ATOM 6732 CE1 TYR D 394 137.777 0.953 19.858 1.00 31.50 D ATOM 6733 CD2 TYR D 394 136.459 2.704 21.565 1.00 31.89 D ATOM 6734 CE2 TYR D 394 137.104 3.189 20.445 1.00 33.06 D ATOM 6735 CZ TYR D 394 137.762 2.316 19.594 1.00 33.32 D ATOM 6736 OH TYR D 394 138.406 2.827 18.492 1.00 33.69 D ATOM 6737 C TYR D 394 134.554 −0.956 24.224 1.00 32.16 D ATOM 6738 O TYR D 394 133.692 −0.582 25.016 1.00 33.01 D ATOM 6739 N VAL D 395 135.359 −1.970 24.481 1.00 31.18 D ATOM 6740 CA VAL D 395 135.307 −2.636 25.767 1.00 30.34 D ATOM 6741 CB VAL D 395 134.724 −4.036 25.689 1.00 32.30 D ATOM 6742 CG1 VAL D 395 134.537 −4.571 27.092 1.00 30.09 D ATOM 6743 CG2 VAL D 395 133.388 −4.017 24.945 1.00 32.97 D ATOM 6744 C VAL D 395 136.751 −2.752 26.150 1.00 29.50 D ATOM 6745 O VAL D 395 137.469 −3.592 25.608 1.00 30.47 D ATOM 6746 N ILE D 396 137.190 −1.895 27.061 1.00 27.33 D ATOM 6747 CA ILE D 396 138.579 −1.929 27.471 1.00 24.79 D ATOM 6748 CB ILE D 396 139.202 −0.529 27.477 1.00 20.54 D ATOM 6749 CG2 ILE D 396 140.724 −0.654 27.607 1.00 18.18 D ATOM 6750 CG1 ILE D 396 138.779 0.231 26.222 1.00 19.10 D ATOM 6751 CD1 ILE D 396 137.698 1.261 26.480 1.00 15.50 D ATOM 6752 C ILE D 396 138.721 −2.532 28.860 1.00 25.91 D ATOM 6753 O ILE D 396 137.839 −2.371 29.709 1.00 25.28 D ATOM 6754 N THR D 397 139.839 −3.228 29.075 1.00 25.38 D ATOM 6755 CA THR D 397 140.133 −3.867 30.352 1.00 24.35 D ATOM 6756 CB THR D 397 139.734 −5.353 30.367 1.00 23.41 D ATOM 6757 OG1 THR D 397 140.542 −6.067 29.425 1.00 22.79 D ATOM 6758 CG2 THR D 397 138.280 −5.530 30.010 1.00 22.25 D ATOM 6759 C THR D 397 141.610 −3.834 30.732 1.00 25.66 D ATOM 6760 O THR D 397 142.492 −3.945 29.876 1.00 25.23 D ATOM 6761 N GLY D 398 141.871 −3.715 32.032 1.00 26.89 D ATOM 6762 CA GLY D 398 143.239 −3.717 32.535 1.00 27.00 D ATOM 6763 C GLY D 398 143.440 −4.892 33.487 1.00 26.90 D ATOM 6764 O GLY D 398 142.464 −5.481 33.951 1.00 26.42 D ATOM 6765 N ALA D 399 144.692 −5.250 33.776 1.00 28.42 D ATOM 6766 CA ALA D 399 144.977 −6.367 34.694 1.00 29.91 D ATOM 6767 CB ALA D 399 144.889 −7.701 33.945 1.00 28.40 D ATOM 6768 C ALA D 399 146.335 −6.265 35.410 1.00 31.06 D ATOM 6769 O ALA D 399 147.208 −5.469 35.041 1.00 29.92 D ATOM 6770 N ASP D 400 146.511 −7.083 36.444 1.00 33.65 D ATOM 6771 CA ASP D 400 147.767 −7.066 37.178 1.00 35.36 D ATOM 6772 CB ASP D 400 147.670 −7.891 38.473 1.00 37.51 D ATOM 6773 CG ASP D 400 148.845 −7.626 39.429 1.00 42.78 D ATOM 6774 OD1 ASP D 400 149.073 −6.446 39.813 1.00 42.00 D ATOM 6775 OD2 ASP D 400 149.544 −8.603 39.802 1.00 45.77 D ATOM 6776 C ASP D 400 148.818 −7.639 36.237 1.00 34.42 D ATOM 6777 O ASP D 400 149.996 −7.735 36.579 1.00 34.18 D ATOM 6778 N ASP D 401 148.379 −8.014 35.037 1.00 33.68 D ATOM 6779 CA ASP D 401 149.293 −8.550 34.047 1.00 32.54 D ATOM 6780 CB ASP D 401 148.571 −9.554 33.118 1.00 31.92 D ATOM 6781 CG ASP D 401 147.897 −8.910 31.909 1.00 31.59 D ATOM 6782 OD1 ASP D 401 147.579 −7.704 31.945 1.00 30.42 D ATOM 6783 OD2 ASP D 401 147.671 −9.645 30.916 1.00 31.10 D ATOM 6784 C ASP D 401 149.901 −7.372 33.293 1.00 32.98 D ATOM 6785 O ASP D 401 150.551 −7.539 32.266 1.00 33.47 D ATOM 6786 N LYS D 402 149.699 −6.180 33.854 1.00 33.97 D ATOM 6787 CA LYS D 402 150.215 −4.921 33.319 1.00 34.64 D ATOM 6788 CB LYS D 402 151.735 −4.825 33.568 1.00 33.75 D ATOM 6789 CG LYS D 402 152.545 −5.988 33.073 1.00 33.34 D ATOM 6790 CD LYS D 402 153.625 −6.377 34.058 1.00 34.65 D ATOM 6791 CE LYS D 402 154.661 −5.300 34.221 1.00 35.08 D ATOM 6792 NZ LYS D 402 155.714 −5.811 35.142 1.00 34.72 D ATOM 6793 C LYS D 402 149.895 −4.650 31.846 1.00 35.07 D ATOM 6794 O LYS D 402 150.606 −3.907 31.167 1.00 35.57 D ATOM 6795 N MSE D 403 148.809 −5.238 31.360 1.00 37.46 D ATOM 6796 CA MSE D 403 148.389 −5.066 29.966 1.00 39.42 D ATOM 6797 CB MSE D 403 148.429 −6.405 29.210 1.00 40.61 D ATOM 6798 CG MSE D 403 149.792 −7.054 29.119 1.00 42.82 D ATOM 6799 SE MSE D 403 150.956 −5.997 28.018 1.00 47.96 D ATOM 6800 CE MSE D 403 152.415 −5.649 29.261 1.00 46.83 D ATOM 6801 C MSE D 403 146.970 −4.518 29.882 1.00 39.22 D ATOM 6802 O MSE D 403 146.140 −4.767 30.761 1.00 41.64 D ATOM 6803 N ILE D 404 146.691 −3.797 28.802 1.00 37.92 D ATOM 6804 CA ILE D 404 145.372 −3.216 28.582 1.00 35.96 O ATOM 6805 CB ILE D 404 145.455 −1.675 28.574 1.00 34.69 O ATOM 6806 CG2 ILE D 404 144.114 −1.082 28.156 1.00 33.19 D ATOM 6807 CG1 ILE D 404 145.880 −1.186 29.962 1.00 33.10 D ATOM 6808 CO1 ILE D 404 146.272 0.266 29.999 1.00 31.33 O ATOM 6809 C ILE D 404 144.788 −3.709 27.251 1.00 35.14 D ATOM 6810 O ILE D 404 145.304 −3.392 26.193 1.00 34.48 O ATOM 6811 N ARG D 405 143.709 −4.482 27.325 1.00 34.81 D ATOM 6812 CA ARG D 405 143.046 −5.027 26.151 1.00 34.51 O ATOM 6813 CB ARG D 405 142.428 −6.373 26.494 1.00 34.25 O ATOM 6814 CG ARG D 405 143.353 −7.285 27.227 1.00 34.29 O ATOM 6815 CD ARG D 405 144.147 −8.101 26.302 1.00 33.92 O ATOM 6816 NE ARG D 405 143.362 −9.187 25.745 1.00 34.85 O ATOM 6817 CZ ARG D 405 143.844 −10.076 24.882 1.00 37.01 D ATOM 6818 NH1 ARG D 405 145.110 −9.992 24.481 1.00 32.55 D ATOM 6819 NH2 ARG D 405 143.069 −11.063 24.436 1.00 38.58 D ATOM 6820 C ARG D 405 141.931 −4.099 25.668 1.00 35.40 O ATOM 6821 O ARG D 405 141.238 −3.474 26.479 1.00 36.54 D ATOM 6822 N VAL D 406 141.749 −4.041 24.349 1.00 35.29 D ATOM 6823 CA VAL D 406 140.719 −3.214 23.719 1.00 34.73 D ATOM 6824 CB VAL D 406 141.332 −2.093 22.879 1.00 35.48 D ATOM 6825 CG1 VAL D 406 140.229 −1.244 22.275 1.00 35.19 D ATOM 6826 CG2 VAL D 406 142.275 −1.253 23.737 1.00 35.51 O ATOM 6827 C VAL D 406 139.921 −4.085 22.780 1.00 34.43 O ATOM 6828 O VAL D 406 140.500 −4.664 21.874 1.00 34.33 D ATOM 6829 N TYR D 407 138.603 −4.160 22.977 1.00 34.53 D ATOM 6830 CA TYR D 407 137.739 −4.985 22.124 1.00 34.18 D ATOM 6831 CB TYR D 407 137.059 −6.091 22.937 1.00 33.29 D ATOM 6832 CG TYR D 407 137.966 −6.948 23.781 1.00 33.16 D ATOM 6833 CD1 TYR D 407 138.423 −6.509 25.026 1.00 32.93 D ATOM 6834 CE1 TYR D 407 139.255 −7.313 25.802 1.00 33.43 D ATOM 6835 CD2 TYR D 407 138.362 −8.206 23.335 1.00 31.85 D ATOM 6836 CE2 TYR D 407 139.189 −9.013 24.091 1.00 31.74 D ATOM 6837 CZ TYR D 407 139.637 −8.572 25.320 1.00 33.54 O ATOM 6838 OH TYR D 407 140.485 −9.378 26.052 1.00 34.77 D ATOM 6839 C TYR D 407 136.635 −4.194 21.417 1.00 34.58 D ATOM 6840 O TYR D 407 136.246 −3.117 21.864 1.00 35.32 D ATOM 6841 N ASP D 408 136.122 −4.775 20.332 1.00 35.38 D ATOM 6842 CA ASP D 408 135.043 −4.221 19.501 1.00 35.74 D ATOM 6843 CB ASP D 408 135.302 −4.625 18.038 1.00 38.38 D ATOM 6844 CG ASP D 408 134.214 −4.143 17.066 1.00 40.45 D ATOM 6845 OD1 ASP D 408 133.015 −4.143 17.433 1.00 41.61 D ATOM 6846 OD2 ASP D 408 134.563 −3.781 15.917 1.00 39.05 D ATOM 6847 C ASP D 408 133.685 −4.788 19.965 1.00 35.67 D ATOM 6848 O ASP D 408 133.413 −5.980 19.799 1.00 35.45 D ATOM 6849 N SER D 409 132.829 −3.934 20.519 1.00 36.24 D ATOM 6850 CA SER D 409 131.510 −4.351 21.021 1.00 37.97 D ATOM 6851 CB SER D 409 130.779 −3.160 21.623 1.00 39.00 D ATOM 6852 OG SER D 409 131.590 −2.452 22.533 1.00 42.40 D ATOM 6853 C SER D 409 130.594 −4.953 19.968 1.00 39.04 D ATOM 6854 O SER D 409 129.915 −5.958 20.216 1.00 38.64 D ATOM 6855 N ILE D 410 130.565 −4.295 18.807 1.00 40.27 D ATOM 6856 CA ILE D 410 129.740 −4.695 17.658 1.00 41.19 D ATOM 6857 CB ILE D 410 129.743 −3.613 16.553 1.00 42.29 D ATOM 6858 CG2 ILE D 410 128.654 −3.904 15.539 1.00 41.48 D ATOM 6859 CG1 ILE D 410 129.507 −2.227 17.162 1.00 43.94 D ATOM 6860 CD1 ILE D 410 129.838 −1.089 16.202 1.00 43.04 D ATOM 6861 C ILE D 410 130.244 −5.996 17.038 1.00 40.21 D ATOM 6862 O ILE D 410 129.616 −7.041 17.170 1.00 40.47 D ATOM 6863 N ASN D 411 131.385 −5.945 16.370 1.00 38.97 D ATOM 6864 CA ASN D 411 131.900 −7.153 15.769 1.00 39.16 D ATOM 6865 CB ASN D 411 133.158 −6.848 14.985 1.00 41.69 D ATOM 6866 CG ASN D 411 132.943 −5.731 13.995 1.00 43.77 D ATOM 6867 OD1 ASN D 411 131.889 −5.649 13.355 1.00 43.07 D ATOM 6868 ND2 ASN D 411 133.938 −4.866 13.855 1.00 45.58 D ATOM 6869 C ASN D 411 132.178 −8.213 16.805 1.00 38.20 D ATOM 6870 O ASN D 411 132.364 −9.377 16.458 1.00 36.34 D ATOM 6871 N LYS D 412 132.197 −7.800 18.074 1.00 37.74 D ATOM 6872 CA LYS D 412 132.451 −8.693 19.211 1.00 36.63 D ATOM 6873 CB LYS D 412 131.300 −9.690 19.338 1.00 35.83 D ATOM 6874 CG LYS D 412 129.936 −9.018 19.314 1.00 35.16 D ATOM 6875 CD LYS D 412 128.805 −10.011 19.175 1.00 34.88 D ATOM 6876 CE LYS D 412 127.483 −9.278 19.119 1.00 36.26 D ATOM 6877 NZ LYS D 412 126.321 −10.211 19.101 1.00 37.05 D ATOM 6878 C LYS D 412 133.776 −9.442 19.066 1.00 36.14 D ATOM 6879 O LYS D 412 133.828 −10.659 19.227 1.00 35.34 D ATOM 6880 N LYS D 413 134.845 −8.707 18.772 1.00 36.48 D ATOM 6881 CA LYS D 413 136.161 −9.314 18.597 1.00 38.12 D ATOM 6882 CB LYS D 413 136.440 −9.573 17.118 1.00 37.83 D ATOM 6883 CG LYS D 413 136.378 −8.322 16.257 1.00 41.43 D ATOM 6884 CD LYS D 413 136.964 −8.566 14.853 1.00 44.72 D ATOM 6885 CE LYS D 413 136.674 −7.400 13.885 1.00 46.65 D ATOM 6886 NZ LYS D 413 137.132 −6.056 14.371 1.00 47.55 D ATOM 6887 C LYS D 413 137.303 −8.471 19.159 1.00 38.78 D ATOM 6888 O LYS D 413 137.244 −7.242 19.151 1.00 38.60 D ATOM 6889 N PHE D 414 138.348 −9.149 19.630 1.00 38.98 D ATOM 6890 CA PHE D 414 139.520 −8.489 20.191 1.00 38.98 D ATOM 6891 CB PHE D 414 140.513 −9.528 20.715 1.00 39.56 D ATOM 6892 CG PHE D 414 141.908 −8.997 20.902 1.00 41.07 D ATOM 6893 CD1 PHE D 414 142.184 −8.046 21.874 1.00 43.51 D ATOM 6894 CD2 PHE D 414 142.949 −9.454 20.110 1.00 41.71 D ATOM 6895 CE1 PHE D 414 143.488 −7.557 22.058 1.00 44.32 D ATOM 6896 CE2 PHE D 414 144.251 −8.973 20.287 1.00 43.60 D ATOM 6897 CZ PHE D 414 144.519 −8.022 21.264 1.00 42.78 D ATOM 6898 C PHE D 414 140.208 −7.620 19.157 1.00 39.17 D ATOM 6899 O PHE D 414 140.529 −8.083 18.068 1.00 40.84 D ATOM 6900 N LEU D 415 140.430 −6.359 19.506 1.00 38.34 D ATOM 6901 CA LEU D 415 141.099 −5.434 18.617 1.00 37.48 D ATOM 6902 CB LEU D 415 140.555 −4.026 18.815 1.00 37.15 D ATOM 6903 CG LEU D 415 139.163 −3.792 18.224 1.00 38.52 D ATOM 6904 CD1 LEU D 415 138.737 −2.351 18.453 1.00 39.38 D ATOM 6905 CD2 LEU D 415 139.191 −4.091 16.736 1.00 39.17 D ATOM 6906 C LEU D 415 142.611 −5.451 18.832 1.00 37.67 D ATOM 6907 O LEU D 415 143.328 −6.171 18.138 1.00 38.98 D ATOM 6908 N LEU D 416 143.097 −4.681 19.799 1.00 35.95 D ATOM 6909 CA LEU D 416 144.528 −4.611 20.052 1.00 34.61 D ATOM 6910 CB LEU D 416 145.102 −3.394 19.317 1.00 32.51 D ATOM 6911 CG LEU D 416 144.656 −2.045 19.880 1.00 30.50 D ATOM 6912 CD1 LEU D 416 145.700 −1.579 20.853 1.00 31.53 D ATOM 6913 CD2 LEU D 416 144.470 −1.017 18.789 1.00 30.55 D ATOM 6914 C LEU D 416 144.865 −4.519 21.545 1.00 35.53 D ATOM 6915 O LEU D 416 144.013 −4.200 22.364 1.00 36.55 D ATOM 6916 N GLN D 417 146.116 −4.791 21.891 1.00 35.81 D ATOM 6917 CA GLN D 417 146.547 −4.716 23.271 1.00 35.57 D ATOM 6918 CB GLN D 417 147.254 −6.007 23.671 1.00 37.43 D ATOM 6919 CG GLN D 417 147.625 −6.074 25.145 1.00 39.62 D ATOM 6920 CD GLN D 417 148.512 −7.253 25.464 1.00 41.04 D ATOM 6921 OE1 CLN D 417 149.615 −7.378 24.914 1.00 43.24 D ATOM 6922 NE2 GLN D 417 148.046 −8.128 26.358 1.00 40.41 D ATOM 6923 C GLN D 417 147.506 −3.532 23.450 1.00 35.61 D ATOM 6924 O GLN D 417 148.374 −3.297 22.605 1.00 35.43 D ATOM 6925 N LEU D 418 147.337 −2.798 24.551 1.00 35.15 D ATOM 6926 CA LEU D 418 148.166 −1.644 24.885 1.00 33.41 D ATOM 6927 CB LEU D 418 147.315 −0.523 25.429 1.00 31.33 D ATOM 6928 CG LEU D 418 146.413 0.034 24.359 1.00 31.84 D ATOM 6929 CD1 LEU D 418 145.508 1.119 24.943 1.00 33.02 D ATOM 6930 CD2 LEU D 418 147.293 0.595 23.253 1.00 33.13 D ATOM 6931 C LEU D 418 149.180 −2.006 25.939 1.00 33.92 D ATOM 6932 O LEU D 418 148.811 −2.281 27.076 1.00 33.63 D ATOM 6933 N SER D 419 150.458 −1.991 25.572 1.00 35.50 D ATOM 6934 CA SER D 419 151.529 −2.323 26.518 1.00 35.75 D ATOM 6935 CB SER D 419 152.504 −3.304 25.889 1.00 36.24 D ATOM 6936 OG SER D 419 153.366 −2.611 25.006 1.00 39.10 D ATOM 6937 C SER D 419 152.286 −1.060 26.903 1.00 34.65 D ATOM 6938 O SER D 419 152.148 −0.036 26.243 1.00 35.71 D ATOM 6939 N GLY D 420 153.082 −1.132 27.969 1.00 34.21 D ATOM 6940 CA GLY D 420 153.845 0.030 28.407 1.00 32.81 D ATOM 6941 C GLY D 420 154.127 0.063 29.904 1.00 32.19 D ATOM 6942 O GLY D 420 155.277 0.111 30.334 1.00 32.95 D ATOM 6943 N HIS D 421 153.057 0.038 30.690 1.00 32.53 D ATOM 6944 CA HIS D 421 153.116 0.056 32.142 1.00 31.89 D ATOM 6945 CB HIS D 421 151.744 −0.233 32.728 1.00 28.17 D ATOM 6946 CG HIS D 421 150.862 0.972 32.856 1.00 26.59 D ATOM 6947 CD2 HIS D 421 149.677 1.270 32.274 1.00 23.86 D ATOM 6948 ND1 HIS D 421 151.123 1.998 33.738 1.00 24.07 D ATOM 6949 CE1 HIS D 421 150.133 2.872 33.699 1.00 24.39 D ATOM 6950 NE2 HIS D 421 149.243 2.454 32.818 1.00 22.81 D ATOM 6951 C HIS D 421 154.082 −0.966 32.714 1.00 34.84 D ATOM 6952 O HIS D 421 154.005 −2.162 32.399 1.00 35.95 D ATOM 6953 N ASP D 422 154.973 −0.487 33.580 1.00 37.06 D ATOM 6954 CA ASP D 422 155.969 −1.328 34.241 1.00 37.22 D ATOM 6955 CB ASP D 422 157.181 −0.481 34.655 1.00 37.19 D ATOM 6956 CG ASP D 422 157.811 0.261 33.479 1.00 38.07 D ATOM 6957 OD1 ASP D 422 158.398 −0.414 32.605 1.00 36.97 D ATOM 6958 OD2 ASP D 422 157.716 1.519 33.426 1.00 39.00 D ATOM 6959 C ASP D 422 155.331 −1.974 35.468 1.00 37.57 D ATOM 6960 O ASP D 422 155.947 −2.791 36.155 1.00 38.18 D ATOM 6961 N GLY D 423 154.089 −1.584 35.735 1.00 38.03 D ATOM 6962 CA GLY D 423 153.357 −2.135 36.862 1.00 37.36 D ATOM 6963 C GLY D 423 151.963 −2.599 36.451 1.00 36.40 D ATOM 6964 O GLY D 423 151.496 −2.282 35.358 1.00 37.00 D ATOM 6965 N GLY D 424 151.297 −3.361 37.311 1.00 35.05 D ATOM 6966 CA GLY D 424 149.965 −3.823 36.984 1.00 33.45 D ATOM 6967 C GLY D 424 149.032 −2.637 36.920 1.00 33.03 D ATOM 6968 O GLY D 424 149.183 −1.692 37.687 1.00 32.43 D ATOM 6969 N VAL D 425 148.074 −2.685 36.004 1.00 33.29 D ATOM 6970 CA VAL D 425 147.112 −1.602 35.826 1.00 34.26 D ATOM 6971 CB VAL D 425 146.545 −1.623 34.420 1.00 34.93 D ATOM 6972 CG1 VAL D 425 145.785 −0.328 34.150 1.00 37.13 D ATOM 6973 CG2 VAL D 425 147.661 −1.843 33.433 1.00 34.83 D ATOM 6974 C VAL D 425 145.955 −1.776 36.795 1.00 33.41 D ATOM 6975 O VAL D 425 145.473 −2.880 36.975 1.00 33.61 D ATOM 6976 N TRP D 426 145.493 −0.700 37.410 1.00 32.49 D ATOM 6977 CA TRP D 426 144.395 −0.837 38.343 1.00 32.03 D ATOM 6978 CB TRP D 426 144.952 −0.866 39.774 1.00 30.72 D ATOM 6979 CG TRP D 426 145.618 −2.192 40.132 1.00 29.46 D ATOM 6980 CD2 TRP D 426 145.011 −3.288 40.834 1.00 27.59 D ATOM 6981 CE2 TRP D 426 145.982 −4.311 40.937 1.00 25.67 D ATOM 6982 CE3 TRP D 426 143.738 −3.502 41.390 1.00 27.62 D ATOM 6983 CD1 TRP D 426 146.903 −2.592 39.838 1.00 28.36 D ATOM 6984 NE1 TRP D 426 147.122 −3.863 40.321 1.00 26.42 D ATOM 6985 CZ2 TRP D 426 145.720 −5.527 41.572 1.00 23.76 D ATOM 6986 CZ3 TRP D 426 143.477 −4.712 42.021 1.00 25.66 D ATOM 6987 CH2 TRP D 426 144.467 −5.711 42.108 1.00 24.10 D ATOM 6988 C TRP D 426 143.291 0.224 38.190 1.00 32.39 D ATOM 6989 O TRP D 426 142.270 0.182 38.876 1.00 32.60 D ATOM 6990 N ALA D 427 143.483 1.164 37.275 1.00 31.70 D ATOM 6991 CA ALA D 427 142.489 2.201 37.060 1.00 32.14 D ATOM 6992 CB ALA D 427 142.699 3.330 38.059 1.00 30.77 D ATOM 6993 C ALA D 427 142.544 2.749 35.631 1.00 32.54 D ATOM 6994 O ALA D 427 143.610 3.128 35.148 1.00 33.11 D ATOM 6995 N LEU D 428 141.403 2.763 34.949 1.00 31.96 D ATOM 6996 CA LEU D 428 141.362 3.298 33.605 1.00 31.52 D ATOM 6997 CB LEU D 428 141.879 2.273 32.591 1.00 30.47 D ATOM 6998 CG LEU D 428 141.523 0.793 32.619 1.00 25.70 D ATOM 6999 CD1 LEU D 428 140.061 0.566 32.426 1.00 26.95 D ATOM 7000 CD2 LEU D 428 142.302 0.127 31.520 1.00 26.15 D ATOM 7001 C LEU D 428 139.998 3.823 33.185 1.00 32.41 D ATOM 7002 O LEU D 428 139.015 3.092 33.159 1.00 31.99 D ATOM 7003 N LYS D 429 139.970 5.117 32.874 1.00 34.44 D ATOM 7004 CA LYS D 429 138.779 5.846 32.441 1.00 36.04 D ATOM 7005 CE LYS D 429 138.655 7.149 33.247 1.00 36.79 D ATOM 7006 CG LYS D 429 137.379 7.954 33.000 1.00 41.16 D ATOM 7007 CD LYS D 429 136.228 7.499 33.914 1.00 44.67 D ATOM 7008 CE LYS D 429 134.828 7.936 33.399 1.00 47.43 D ATOM 7009 NZ LYS D 429 134.385 7.223 32.133 1.00 49.62 D ATOM 7010 C LYS D 429 138.944 6.184 30.951 1.00 35.80 D ATOM 7011 O LYS D 429 139.982 6.698 30.531 1.00 35.22 D ATOM 7012 N TYR D 430 137.926 5.888 30.152 1.00 36.71 D ATOM 7013 CA TYR D 430 137.962 6.183 28.719 1.00 38.50 D ATOM 7014 CE TYR D 430 137.142 5.152 27.936 1.00 38.31 D ATOM 7015 CG TYR D 430 136.840 5.560 26.501 1.00 38.68 D ATOM 7016 CD1 TYR D 430 135.713 6.331 26.192 1.00 38.18 D ATOM 7017 CE1 TYR D 430 135.427 6.702 24.875 1.00 37.22 D ATOM 7018 CD2 TYR D 430 137.680 5.173 25.449 1.00 39.59 D ATOM 7019 CE2 TYR D 430 137.403 5.542 24.126 1.00 38.38 D ATOM 7020 CZ TYR D 430 136.275 6.303 23.853 1.00 38.21 D ATOM 7021 OH TYR D 430 135.983 6.646 22.557 1.00 37.82 D ATOM 7022 C TYR D 430 137.401 7.574 28.427 1.00 39.86 D ATOM 7023 O TYR D 430 136.344 7.931 28.934 1.00 39.99 D ATOM 7024 N ALA D 431 138.109 8.349 27.607 1.00 40.69 D ATOM 7025 CA ALA D 431 137.660 9.688 27.227 1.00 41.42 D ATOM 7026 CB ALA D 431 138.790 10.695 27.407 1.00 40.10 D ATOM 7027 C ALA D 431 137.208 9.641 25.763 1.00 43.09 D ATOM 7028 O ALA D 431 137.842 8.998 24.916 1.00 43.69 D ATOM 7029 N HIS D 432 136.108 10.321 25.465 1.00 42.71 D ATOM 7030 CA HIS D 432 135.584 10.340 24.102 1.00 43.16 D ATOM 7031 CB HIS D 432 134.468 11.383 23.966 1.00 47.95 D ATOM 7032 CG HIS D 432 133.942 11.523 22.566 1.00 53.08 D ATOM 7033 CD2 HIS D 432 133.728 12.622 21.801 1.00 53.58 D ATOM 7034 ND1 HIS D 432 133.594 10.439 21.787 1.00 53.70 D ATOM 7035 CE1 HIS D 432 133.192 10.865 20.601 1.00 54.74 D ATOM 7036 NE2 HIS D 432 133.265 12.184 20.584 1.00 54.71 D ATOM 7037 C HIS D 432 136.646 10.636 23.052 1.00 40.32 D ATOM 7038 O HIS D 432 137.420 11.573 23.201 1.00 40.89 D ATOM 7039 N GLY D 433 136.669 9.852 21.980 1.00 37.59 D ATOM 7040 CA GLY D 433 137.640 10.095 20.926 1.00 36.16 D ATOM 7041 C GLY D 433 138.701 9.029 20.850 1.00 34.81 D ATOM 7042 O GLY D 433 139.697 9.177 20.143 1.00 32.92 D ATOM 7043 N GLY D 434 138.474 7.948 21.588 1.00 36.25 D ATOM 7044 CA GLY D 434 139.412 6.841 21.617 1.00 36.22 D ATOM 7045 C GLY D 434 140.580 7.079 22.557 1.00 36.76 D ATOM 7046 O GLY D 434 141.559 6.338 22.493 1.00 37.12 D ATOM 7047 N ILE D 435 140.469 8.106 23.411 1.00 37.42 D ATOM 7048 CA ILE D 435 141.501 8.478 24.397 1.00 37.95 D ATOM 7049 CB ILE D 435 141.424 9.992 24.784 1.00 39.16 D ATOM 7050 CG2 ILE D 435 142.684 10.430 25.539 1.00 37.49 D ATOM 7051 CG1 ILE D 435 141.328 10.839 23.519 1.00 39.15 D ATOM 7052 CD1 ILE D 435 142.476 10.580 22.572 1.00 38.06 D ATOM 7053 C ILE D 435 141.273 7.662 25.658 1.00 37.16 D ATOM 7054 O ILE D 435 140.130 7.426 26.059 1.00 36.94 D ATOM 7055 N LEU D 436 142.360 7.251 26.297 1.00 35.58 D ATOM 7056 CA LEU D 436 142.243 6.427 27.481 1.00 34.59 D ATOM 7057 CB LEU D 436 142.354 4.980 27.046 1.00 35.11 D ATOM 7058 CG LEU D 436 141.894 3.866 27.965 1.00 35.32 D ATOM 7059 CD1 LEU D 436 142.000 2.560 27.178 1.00 34.07 D ATOM 7060 CD2 LEU D 436 142.727 3.819 29.234 1.00 35.01 D ATOM 7061 C LEU D 436 143.309 6.742 28.511 1.00 34.64 D ATOM 7062 O LEU D 436 144.495 6.786 28.195 1.00 35.84 D ATOM 7063 N VAL D 437 142.891 6.960 29.750 1.00 33.63 D ATOM 7064 CA VAL D 437 143.854 7.244 30.801 1.00 32.09 D ATOM 7065 CB VAL D 437 143.484 8.519 31.575 1.00 31.66 D ATOM 7066 CG1 VAL D 437 144.624 8.902 32.506 1.00 32.49 D ATOM 7067 CG2 VAL D 437 143.172 9.650 30.608 1.00 31.31 D ATOM 7068 C VAL D 437 143.887 6.058 31.764 1.00 31.94 D ATOM 7069 O VAL D 437 142.845 5.454 32.047 1.00 31.55 D ATOM 7070 N SER D 438 145.080 5.707 32.246 1.00 29.85 D ATOM 7071 CA SER D 438 145.201 4.597 33.189 1.00 26.33 D ATOM 7072 CB SER D 438 145.601 3.302 32.480 1.00 25.65 D ATOM 7073 OG SER D 438 146.858 3.426 31.852 1.00 26.66 D ATOM 7074 C SER D 438 146.156 4.853 34.336 1.00 23.90 D ATOM 7075 O SER D 438 146.977 5.765 34.294 1.00 21.89 D ATOM 7076 N GLY D 439 146.019 4.025 35.366 1.00 23.29 D ATOM 7077 CA GLY D 439 146.835 4.130 36.563 1.00 23.55 D ATOM 7078 C GLY D 439 147.396 2.783 36.962 1.00 23.12 D ATOM 7079 O GLY D 439 146.725 1.748 36.883 1.00 22.22 D ATOM 7080 N SER D 440 148.634 2.800 37.429 1.00 23.85 D ATOM 7081 CA SER D 440 149.302 1.562 37.786 1.00 25.71 D ATOM 7082 CB SER D 440 150.244 1.169 36.630 1.00 24.70 D ATOM 7083 OG SER D 440 151.145 0.129 36.979 1.00 23.47 D ATOM 7084 C SER D 440 150.078 1.620 39.099 1.00 26.18 D ATOM 7085 O SER D 440 150.112 2.651 39.793 1.00 26.21 D ATOM 7086 N THR D 441 150.695 0.481 39.413 1.00 27.38 D ATOM 7087 CA THR D 441 151.521 0.308 40.593 1.00 27.39 D ATOM 7088 CB THR D 441 151.676 −1.165 40.968 1.00 28.12 D ATOM 7089 OG1 THR D 441 152.519 −1.810 40.004 1.00 27.63 D ATOM 7090 CG2 THR D 441 150.310 −1.858 41.003 1.00 28.73 D ATOM 7091 C THR D 441 152.903 0.847 40.237 1.00 28.31 D ATOM 7092 O THR D 441 153.768 0.906 41.090 1.00 29.00 D ATOM 7093 N ASP D 442 153.116 1.234 38.980 1.00 29.46 D ATOM 7094 CA ASP D 442 154.402 1.796 38.603 1.00 31.38 D ATOM 7095 CB ASP D 442 154.724 1.551 37.126 1.00 33.65 D ATOM 7096 CG ASP D 442 153.695 2.167 36.185 1.00 35.87 D ATOM 7097 OD1 ASP D 442 152.845 2.962 36.680 1.00 35.07 D ATOM 7098 OD2 ASP D 442 153.753 1.860 34.959 1.00 34.85 D ATOM 7099 C ASP D 442 154.351 3.287 38.857 1.00 31.58 D ATOM 7100 O ASP D 442 155.161 4.049 38.334 1.00 31.31 D ATOM 7101 N ARG D 443 153.360 3.700 39.635 1.00 31.79 D ATOM 7102 CA ARG D 443 153.191 5.100 39.983 1.00 31.82 D ATOM 7103 CB ARG D 443 154.413 5.569 40.760 1.00 28.96 D ATOM 7104 CG ARG D 443 154.805 4.604 41.846 1.00 26.68 D ATOM 7105 CD ARG D 443 156.056 5.065 42.541 1.00 25.25 D ATOM 7106 NE ARG D 443 156.496 4.111 43.541 1.00 26.33 D ATOM 7107 CZ ARG D 443 157.552 4.303 44.319 1.00 27.22 D ATOM 7108 NH1 ARG D 443 158.250 5.419 44.192 1.00 28.58 D ATOM 7109 NH2 ARG D 443 157.916 3.388 45.213 1.00 26.32 D ATOM 7110 C ARG D 443 152.955 6.016 38.783 1.00 32.05 D ATOM 7111 O ARG D 443 152.975 7.243 38.917 1.00 32.48 D ATOM 7112 N THR D 444 152.705 5.439 37.616 1.00 31.82 D ATOM 7113 CA THR D 444 152.486 6.283 36.459 1.00 32.99 D ATOM 7114 CB THR D 444 153.335 5.824 35.246 1.00 32.98 D ATOM 7115 OG1 THR D 444 152.768 4.643 34.657 1.00 30.88 D ATOM 7116 CG2 THR D 444 154.757 5.549 35.680 1.00 31.91 D ATOM 7117 C THR D 444 151.036 6.451 36.000 1.00 34.38 D ATOM 7118 O THR D 444 150.182 5.570 36.164 1.00 34.02 D ATOM 7119 N VAL D 445 150.784 7.623 35.432 1.00 35.02 D ATOM 7120 CA VAL D 445 149.492 7.992 34.888 1.00 35.88 D ATOM 7121 CB VAL D 445 149.049 9.384 35.406 1.00 34.38 D ATOM 7122 CG1 VAL D 445 147.839 9.871 34.640 1.00 33.91 D ATOM 7123 CG2 VAL D 445 148.747 9.312 36.893 1.00 33.31 D ATOM 7124 C VAL D 445 149.787 8.067 33.392 1.00 38.00 D ATOM 7125 O VAL D 445 150.648 8.841 32.969 1.00 40.09 D ATOM 7126 N ARG D 446 149.116 7.256 32.583 1.00 38.70 D ATOM 7127 CA ARG D 446 149.390 7.299 31.152 1.00 40.25 D ATOM 7128 CB ARG D 446 150.102 6.016 30.707 1.00 40.97 D ATOM 7129 CG ARG D 446 151.387 5.796 31.448 1.00 42.38 D ATOM 7130 CD ARG D 446 152.190 4.636 30.925 1.00 44.42 D ATOM 7131 NE ARG D 446 153.302 4.360 31.835 1.00 48.85 D ATOM 7132 CZ ARG D 446 154.291 3.506 31.588 1.00 50.95 D ATOM 7133 NH1 ARG D 446 154.316 2.834 30.442 1.00 52.13 D ATOM 7134 NH2 ARG D 446 155.251 3.320 32.490 1.00 51.46 D ATOM 7135 C ARG D 446 148.155 7.527 30.296 1.00 40.71 D ATOM 7136 O ARG D 446 147.050 7.083 30.635 1.00 39.57 D ATOM 7137 N VAL D 447 148.357 8.253 29.195 1.00 40.90 D ATOM 7138 CA VAL D 447 147.293 8.552 28.237 1.00 41.54 D ATOM 7139 CB VAL D 447 147.260 10.037 27.849 1.00 40.47 D ATOM 7140 CG1 VAL D 447 146.043 10.306 26.981 1.00 38.69 D ATOM 7141 CG2 VAL D 447 147.226 10.895 29.100 1.00 40.93 D ATOM 7142 C VAL D 447 147.566 7.735 26.991 1.00 42.31 D ATOM 7143 O VAL D 447 148.689 7.712 26.501 1.00 43.98 D ATOM 7144 N TRP D 448 146.549 7.055 26.481 1.00 42.01 D ATOM 7145 CA TRP D 448 146.730 6.234 25.296 1.00 42.06 D ATOM 7146 CB TRP D 448 146.416 4.769 25.625 1.00 40.93 D ATOM 7147 CG TRP D 448 147.108 4.254 26.849 1.00 40.06 D ATOM 7148 CD2 TRP D 448 148.167 3.294 26.890 1.00 39.39 D ATOM 7149 CE2 TRP D 448 148.529 3.127 28.247 1.00 39.74 D ATOM 7150 CE3 TRP D 448 148.846 2.555 25.911 1.00 37.93 D ATOM 7151 CD1 TRP D 448 146.871 4.621 28.145 1.00 39.85 D ATOM 7152 NE1 TRP D 448 147.720 3.949 28.992 1.00 39.87 D ATOM 7153 CZ2 TRP D 448 149.552 2.247 28.653 1.00 38.84 D ATOM 7154 CZ3 TRP D 448 149.860 1.680 26.314 1.00 38.08 D ATOM 7155 CH2 TRP D 448 150.203 1.537 27.679 1.00 37.48 D ATOM 7156 C TRP D 448 145.825 6.705 24.156 1.00 42.74 D ATOM 7157 O TRP D 448 144.933 7.537 24.349 1.00 42.62 D ATOM 7158 N ASP D 449 146.067 6.165 22.967 1.00 43.66 D ATOM 7159 CA ASP D 449 145.265 6.485 21.797 1.00 44.36 D ATOM 7160 CB ASP D 449 146.062 7.368 20.836 1.00 45.33 D ATOM 7161 CG ASP D 449 145.256 7.782 19.616 1.00 46.25 D ATOM 7162 OD1 ASP D 449 145.791 8.522 18.771 1.00 46.26 D ATOM 7163 OD2 ASP D 449 144.088 7.370 19.494 1.00 47.22 D ATOM 7164 C ASP D 449 144.899 5.169 21.119 1.00 44.82 D ATOM 7165 O ASP D 449 145.735 4.551 20.468 1.00 44.81 D ATOM 7166 N ILE D 450 143.653 4.740 21.280 1.00 45.73 D ATOM 7167 CA ILE D 450 143.205 3.484 20.687 1.00 47.64 D ATOM 7168 CB ILE D 450 141.711 3.215 21.000 1.00 46.91 D ATOM 7169 CG2 ILE D 450 141.335 1.820 20.527 1.00 45.80 D ATOM 7170 CG1 ILE D 450 141.455 3.357 22.507 1.00 46.32 D ATOM 7171 CD1 ILE D 450 140.009 3.138 22.920 1.00 46.07 D ATOM 7172 C ILE D 450 143.395 3.516 19.173 1.00 49.71 D ATOM 7173 O ILE D 450 143.890 2.556 18.573 1.00 49.74 D ATOM 7174 N LYS D 451 142.984 4.631 18.571 1.00 51.95 D ATOM 7175 CA LYS D 451 143.092 4.859 17.130 1.00 52.66 D ATOM 7176 CB LYS D 451 142.789 6.329 16.815 1.00 54.03 D ATOM 7177 CG LYS D 451 141.425 6.825 17.283 1.00 54.77 D ATOM 7178 CD LYS D 451 140.315 6.348 16.362 1.00 56.08 D ATOM 7179 CE LYS D 451 138.958 6.853 16.829 1.00 58.40 D ATOM 7180 NZ LYS D 451 138.564 6.293 18.170 1.00 60.81 D ATOM 7181 C LYS D 451 144.519 4.534 16.687 1.00 53.12 D ATOM 7182 O LYS D 451 144.743 3.637 15.875 1.00 52.92 D ATOM 7183 N LYS D 452 145.478 5.279 17.236 1.00 53.06 D ATOM 7184 CA LYS D 452 146.889 5.081 16.922 1.00 53.16 D ATOM 7185 CB LYS D 452 147.727 6.274 17.405 1.00 54.65 D ATOM 7186 CG LYS D 452 147.432 7.608 16.705 1.00 55.78 D ATOM 7187 CD LYS D 452 148.434 8.689 17.106 1.00 54.91 D ATOM 7188 CE LYS D 452 148.269 9.952 16.262 1.00 56.24 D ATOM 7189 NZ LYS D 452 146.931 10.592 16.394 1.00 55.58 D ATOM 7190 C LYS D 452 147.426 3.801 17.565 1.00 52.16 D ATOM 7191 O LYS D 452 148.530 3.352 17.257 1.00 52.14 D ATOM 7192 N GLY D 453 146.646 3.221 18.466 1.00 51.03 D ATOM 7193 CA GLY D 453 147.070 2.000 19.119 1.00 48.98 D ATOM 7194 C GLY D 453 148.425 2.076 19.795 1.00 47.55 D ATOM 7195 O GLY D 453 149.268 1.206 19.598 1.00 48.41 D ATOM 7196 N CYS D 454 148.643 3.111 20.595 1.00 45.89 D ATOM 7197 CA CYS D 454 149.903 3.252 21.306 1.00 45.10 D ATOM 7198 CB CYS D 454 151.007 3.764 20.371 1.00 45.35 D ATOM 7199 SG CYS D 454 151.016 5.592 20.180 1.00 46.05 D ATOM 7200 C CYS D 454 149.733 4.246 22.445 1.00 45.09 D ATOM 7201 O CYS D 454 148.660 4.827 22.632 1.00 43.95 D ATOM 7202 N CYS D 455 150.815 4.443 23.191 1.00 45.72 D ATOM 7203 CA CYS D 455 150.831 5.373 24.307 1.00 46.22 D ATOM 7204 CB CYS D 455 151.663 4.818 25.461 1.00 46.14 D ATOM 7205 SG CYS D 455 151.652 5.917 26.902 1.00 44.91 D ATOM 7206 C CYS D 455 151.412 6.717 23.880 1.00 45.90 D ATOM 7207 O CYS D 455 152.504 6.787 23.328 1.00 45.72 D ATOM 7208 N THR D 456 150.674 7.778 24.160 1.00 46.41 D ATOM 7209 CA THR D 456 151.089 9.114 23.807 1.00 47.30 D ATOM 7210 CB THR D 456 149.878 9.947 23.316 1.00 47.67 D ATOM 7211 OG1 THR D 456 150.170 11.344 23.454 1.00 49.91 D ATOM 7212 CG2 THR D 456 148.633 9.623 24.124 1.00 48.32 D ATOM 7213 C THR D 456 151.767 9.870 24.953 1.00 47.34 D ATOM 7214 O THR D 456 152.722 10.614 24.729 1.00 47.57 D ATOM 7215 N HIS D 457 151.280 9.691 26.177 1.00 46.90 D ATOM 7216 CA HIS D 457 151.850 10.407 27.315 1.00 46.66 D ATOM 7217 CB HIS D 457 150.935 11.569 27.708 1.00 48.78 D ATOM 7218 CG HIS D 457 150.781 12.608 26.639 1.00 52.07 D ATOM 7219 CD2 HIS D 457 149.752 12.884 25.802 1.00 53.00 D ATOM 7220 ND1 HIS D 457 151.768 13.525 26.349 1.00 51.90 D ATOM 7221 CE1 HIS D 457 151.351 14.324 25.383 1.00 53.55 D ATOM 7222 NE2 HIS D 457 150.131 13.957 25.033 1.00 53.69 D ATOM 7223 C HIS D 457 152.101 9.534 28.529 1.00 45.09 D ATOM 7224 O HIS D 457 151.360 8.591 28.797 1.00 46.21 D ATOM 7225 N VAL D 458 153.163 9.864 29.255 1.00 43.08 D ATOM 7226 CA VAL D 458 153.544 9.142 30.462 1.00 40.12 D ATOM 7227 CB VAL D 458 154.847 8.350 30.247 1.00 38.48 D ATOM 7228 CG1 VAL D 458 155.106 7.437 31.430 1.00 36.35 D ATOM 7229 CG2 VAL D 458 154.758 7.554 28.954 1.00 37.80 D ATOM 7230 C VAL D 458 153.761 10.197 31.535 1.00 38.68 D ATOM 7231 O VAL D 458 154.733 10.942 31.474 1.00 38.06 D ATOM 7232 N PHE D 459 152.834 10.267 32.491 1.00 37.03 D ATOM 7233 CA PHE D 459 152.902 11.230 33.588 1.00 35.98 D ATOM 7234 CB PHE D 459 151.526 11.848 33.859 1.00 35.38 D ATOM 7235 CG PHE D 459 151.009 12.705 32.729 1.00 36.52 D ATOM 7236 CD1 PHE D 459 149.643 12.975 32.603 1.00 35.53 D ATOM 7237 CD2 PHE D 459 151.882 13.228 31.773 1.00 36.02 D ATOM 7238 CE1 PHE D 459 149.160 13.748 31.542 1.00 33.32 D ATOM 7239 CE2 PHE D 459 151.404 13.999 30.715 1.00 34.61 D ATOM 7240 CZ PHE D 459 150.040 14.258 30.599 1.00 33.14 D ATOM 7241 C PHE D 459 153.421 10.583 34.858 1.00 35.63 D ATOM 7242 O PHE D 459 152.927 9.540 35.286 1.00 36.76 D ATOM 7243 N GLU D 460 154.436 11.210 35.443 1.00 34.40 D ATOM 7244 CA GLU D 460 155.042 10.731 36.669 1.00 32.85 D ATOM 7245 CB GLD D 460 156.541 10.572 36.501 1.00 31.50 D ATOM 7246 CG GLU D 460 156.912 9.591 35.436 1.00 34.06 D ATOM 7247 CD GLU D 460 158.340 9.146 35.561 1.00 34.99 D ATOM 7248 OE1 GLU D 460 159.177 9.996 35.916 1.00 38.06 D ATOM 7249 OE2 GLU D 460 158.634 7.959 35.305 1.00 34.49 D ATOM 7250 C GLU D 460 154.754 11.770 37.717 1.00 32.81 D ATOM 7251 O GLU D 460 154.506 12.927 37.387 1.00 33.34 D ATOM 7252 N GLY D 461 154.788 11.364 38.982 1.00 33.03 D ATOM 7253 CA GLY D 461 154.503 12.295 40.057 1.00 31.23 D ATOM 7254 C GLY D 461 154.150 11.600 41.354 1.00 30.79 D ATOM 7255 O GLY D 461 154.770 11.857 42.383 1.00 31.55 D ATOM 7256 N HIS D 462 153.151 10.727 41.318 1.00 30.63 D ATOM 7257 CA HIS D 462 152.744 10.016 42.522 1.00 30.77 D ATOM 7258 CB HIS D 462 151.580 9.065 42.209 1.00 30.12 D ATOM 7259 CG HIS D 462 150.254 9.754 42.066 1.00 29.59 D ATOM 7260 CD2 HIS D 462 149.387 9.814 41.026 1.00 29.20 D ATOM 7261 ND1 HIS D 462 149.701 10.520 43.070 1.00 27.98 D ATOM 7262 CE1 HIS D 462 148.555 11.027 42.652 1.00 29.48 D ATOM 7263 NE2 HIS D 462 148.342 10.615 41.415 1.00 29.45 D ATOM 7264 C HIS D 462 153.935 9.233 43.032 1.00 31.13 D ATOM 7265 O HIS D 462 154.687 8.672 42.240 1.00 32.76 D ATOM 7266 N ASN D 463 154.113 9.195 44.349 1.00 31.08 D ATOM 7267 CA ASN D 463 155.239 8.473 44.929 1.00 30.79 D ATOM 7268 CB ASN D 463 155.764 9.212 46.155 1.00 31.33 D ATOM 7269 CG ASN D 463 156.351 10.572 45.806 1.00 33.80 D ATOM 7270 OD1 ASN D 463 156.669 11.368 46.700 1.00 36.56 D ATOM 7271 ND2 ASN D 463 156.500 10.848 44.511 1.00 31.92 D ATOM 7272 C ASN D 463 154.863 7.058 45.300 1.00 30.83 D ATOM 7273 O ASN D 463 155.678 6.319 45.843 1.00 32.01 D ATOM 7274 N SER D 464 153.623 6.685 44.996 1.00 30.09 D ATOM 7275 CA SER D 464 153.099 5.346 45.292 1.00 29.60 D ATOM 7276 CB SER D 464 152.364 5.358 46.630 1.00 31.07 D ATOM 7277 OG SER D 464 153.073 4.621 47.611 1.00 34.87 D ATOM 7278 C SER D 464 152.125 4.900 44.203 1.00 28.55 D ATOM 7279 O SER D 464 151.814 5.656 43.289 1.00 29.29 D ATOM 7280 N THR D 465 151.625 3.676 44.313 1.00 27.12 D ATOM 7281 CA THR D 465 150.675 3.153 43.331 1.00 25.67 D ATOM 7282 CB THR D 465 150.036 1.828 43.817 1.00 23.85 D ATOM 7283 OG1 THR D 465 151.057 0.894 44.197 1.00 24.69 D ATOM 7284 CG2 THR D 465 149.169 1.234 42.742 1.00 22.12 D ATOM 7285 C THR D 465 149.536 4.150 43.089 1.00 26.17 D ATOM 7286 O THR D 465 149.122 4.872 44.001 1.00 27.21 D ATOM 7287 N VAL D 466 149.041 4.197 41.856 1.00 25.63 D ATOM 7288 CA VAL D 466 147.933 5.078 41.506 1.00 24.45 D ATOM 7289 CB VAL D 466 148.003 5.484 39.994 1.00 26.90 D ATOM 7290 CG1 VAL D 466 146.795 6.351 39.597 1.00 27.11 D ATOM 7291 CG2 VAL D 466 149.300 6.240 39.732 1.00 27.75 D ATOM 7292 C VAL D 466 146.740 4.165 41.783 1.00 22.49 D ATOM 7293 O VAL D 466 146.604 3.130 41.148 1.00 19.72 D ATOM 7294 N ARG D 467 145.894 4.543 42.737 1.00 21.80 D ATOM 7295 CA ARG D 467 144.764 3.713 43.121 1.00 21.09 D ATOM 7296 CB ARG D 467 144.529 3.828 44.637 1.00 21.63 D ATOM 7297 CG ARG D 467 143.582 2.778 45.221 1.00 24.03 D ATOM 7298 CD ARG D 467 144.190 1.398 45.033 1.00 25.89 D ATOM 7299 NE ARG D 467 143.247 0.294 45.158 1.00 27.91 D ATOM 7300 CZ ARG D 467 142.283 0.013 44.288 1.00 30.10 D ATOM 7301 NH1 ARG D 467 142.117 0.776 43.214 1.00 32.22 D ATOM 7302 NH2 ARG D 467 141.515 −1.064 44.469 1.00 28.51 D ATOM 7303 C ARG D 467 143.463 3.984 42.370 1.00 21.53 D ATOM 7304 O ARG D 467 142.666 3.071 42.152 1.00 21.18 D ATOM 7305 N CYS D 468 143.240 5.225 41.960 1.00 21.08 D ATOM 7306 CA CYS D 468 142.008 5.538 41.259 1.00 22.04 D ATOM 7307 CB CYS D 468 140.874 5.672 42.282 1.00 22.73 D ATOM 7308 SG CYS D 468 141.036 7.052 43.480 1.00 26.78 D ATOM 7309 C CYS D 468 142.141 6.807 40.433 1.00 22.89 D ATOM 7310 O CYS D 468 143.034 7.617 40.672 1.00 24.06 D ATOM 7311 N LEU D 469 141.247 6.995 39.466 1.00 23.65 D ATOM 7312 CA LEU D 469 141.321 8.189 38.614 1.00 25.22 D ATOM 7313 CB LEU D 469 142.382 7.997 37.512 1.00 25.67 D ATOM 7314 CG LEU D 469 142.191 6.914 36.441 1.00 25.46 D ATOM 7315 CD1 LEU D 469 140.965 7.170 35.605 1.00 24.47 D ATOM 7316 CD2 LEU D 469 143.428 6.891 35.560 1.00 26.81 D ATOM 7317 C LEU D 469 140.005 8.574 37.960 1.00 24.60 D ATOM 7318 O LEU D 469 139.162 7.729 37.690 1.00 24.12 D ATOM 7319 N ASP D 470 139.818 9.853 37.693 1.00 24.30 D ATOM 7320 CA ASP D 470 138.584 10.242 37.043 1.00 24.73 D ATOM 7321 CB ASP D 470 137.540 10.594 38.118 1.00 24.80 D ATOM 7322 CG ASP D 470 136.109 10.685 37.571 1.00 24.84 D ATOM 7323 OD1 ASP D 470 135.842 10.240 36.441 1.00 25.89 D ATOM 7324 OD2 ASP D 470 135.242 11.197 38.296 1.00 23.60 D ATOM 7325 C ASP D 470 138.857 11.409 36.091 1.00 24.57 D ATOM 7326 O ASP D 470 139.863 12.118 36.214 1.00 23.14 D ATOM 7327 N ILE D 471 137.988 11.584 35.110 1.00 24.45 D ATOM 7328 CA ILE D 471 138.184 12.684 34.197 1.00 26.31 D ATOM 7329 CB ILE D 471 138.389 12.210 32.737 1.00 24.06 D ATOM 7330 CG2 ILE D 471 138.861 13.393 31.915 1.00 24.13 D ATOM 7331 CG1 ILE D 471 139.454 11.097 32.656 1.00 22.43 D ATOM 7332 CD1 ILE D 471 139.553 10.449 31.293 1.00 18.18 D ATOM 7333 C ILE D 471 136.971 13.600 34.271 1.00 28.56 D ATOM 7334 O ILE D 471 135.833 13.135 34.280 1.00 30.74 D ATOM 7335 N VAL D 472 137.222 14.901 34.358 1.00 30.47 D ATOM 7336 CA VAL D 472 136.157 15.892 34.433 1.00 31.86 D ATOM 7337 CB VAL D 472 136.105 16.544 35.857 1.00 31.83 D ATOM 7338 CG1 VAL D 472 135.793 15.474 36.896 1.00 30.28 D ATOM 7339 CG2 VAL D 472 137.427 17.231 36.193 1.00 27.41 D ATOM 7340 C VAL D 472 136.369 16.966 33.358 1.00 33.87 D ATOM 7341 O VAL D 472 137.474 17.119 32.826 1.00 34.57 D ATOM 7342 N GLU D 473 135.304 17.692 33.026 1.00 35.69 D ATOM 7343 CA GLU D 473 135.354 18.747 32.004 1.00 37.97 D ATOM 7344 CE GLU D 473 134.565 18.321 30.751 1.00 39.26 D ATOM 7345 CG GLU D 473 134.587 19.326 29.567 1.00 41.82 D ATOM 7346 CD GLU D 473 133.581 18.966 28.455 1.00 41.92 D ATOM 7347 OE1 GLU D 473 133.651 17.853 27.893 1.00 41.68 D ATOM 7348 OE2 GLU D 473 132.712 19.801 28.145 1.00 42.75 D ATOM 7349 C GLU D 473 134.722 19.983 32.620 1.00 38.63 D ATOM 7350 O GLU D 473 133.585 19.944 33.084 1.00 39.66 D ATOM 7351 N TYR D 474 135.464 21.077 32.651 1.00 39.16 D ATOM 7352 CA TYR D 474 134.952 22.311 33.231 1.00 39.98 D ATOM 7353 CB TYR D 474 135.534 22.496 34.630 1.00 39.54 D ATOM 7354 CG TYR D 474 135.126 23.777 35.311 1.00 40.62 D ATOM 7355 CD1 TYR D 474 133.802 24.002 35.686 1.00 40.93 D ATOM 7356 CE1 TYR D 474 133.432 25.174 36.332 1.00 40.40 D ATOM 7357 CD2 TYR D 474 136.072 24.761 35.601 1.00 40.52 D ATOM 7358 CE2 TYR D 474 135.714 25.933 36.243 1.00 40.34 D ATOM 7359 CZ TYR D 474 134.393 26.134 36.604 1.00 40.71 D ATOM 7360 OH TYR D 474 134.025 27.300 37.224 1.00 41.79 D ATOM 7361 C TYR D 474 135.422 23.394 32.277 1.00 39.99 D ATOM 7362 O TYR D 474 136.550 23.339 31.784 1.00 40.02 D ATOM 7363 N LYS D 475 134.551 24.357 31.998 1.00 40.09 D ATOM 7364 CA LYE D 475 134.868 25.438 31.069 1.00 42.55 D ATOM 7365 CE LYE D 475 135.796 26.471 31.723 1.00 43.10 D ATOM 7366 CG LYS D 475 135.185 27.292 32.864 1.00 43.55 D ATOM 7367 CD LYS D 475 136.276 28.148 33.502 1.00 46.85 D ATOM 7368 CE LYE D 475 135.765 29.052 34.623 1.00 48.93 D ATOM 7369 NZ LYE D 475 134.765 30.077 34.181 1.00 49.55 D ATOM 7370 C LYE D 475 135.529 24.888 29.804 1.00 43.23 D ATOM 7371 O LYE D 475 136.556 25.401 29.352 1.00 43.08 D ATOM 7372 N ASN D 476 134.943 23.831 29.248 1.00 44.27 D ATOM 7373 CA ASN D 476 135.449 23.202 28.024 1.00 44.54 D ATOM 7374 CB ASN D 476 135.383 24.180 26.850 1.00 44.94 D ATOM 7375 CG ASN D 476 134.054 24.135 26.140 1.00 44.85 D ATOM 7376 OD1 ASN D 476 133.040 24.596 26.665 1.00 44.09 D ATOM 7377 ND2 ASN D 476 134.048 23.565 24.934 1.00 45.89 D ATOM 7378 C ASN D 476 136.841 22.591 28.077 1.00 44.03 D ATOM 7379 O ASN D 476 137.403 22.230 27.036 1.00 44.45 D ATOM 7380 N ILE D 477 137.400 22.474 29.280 1.00 43.98 D ATOM 7381 CA ILE D 477 138.722 21.860 29.459 1.00 42.39 D ATOM 7382 CB ILE D 477 139.681 22.744 30.260 1.00 42.82 D ATOM 7383 CG2 ILE D 477 141.024 22.052 30.387 1.00 43.06 D ATOM 7384 CG1 ILE D 477 139.842 24.097 29.583 1.00 42.36 D ATOM 7385 CD1 ILE D 477 140.465 25.135 30.486 1.00 41.94 D ATOM 7386 C ILE D 477 138.528 20.578 30.249 1.00 41.19 D ATOM 7387 O ILE D 477 137.805 20.560 31.253 1.00 40.43 D ATOM 7388 N LYS D 478 139.166 19.511 29.777 1.00 38.84 D ATOM 7389 CA LYS D 478 139.078 18.212 30.428 1.00 36.96 D ATOM 7390 CB LYS D 478 139.070 17.085 29.394 1.00 35.75 D ATOM 7391 CG LYS D 478 137.740 16.932 28.687 1.00 35.23 D ATOM 7392 CD LYS D 478 137.557 15.519 28.160 1.00 32.30 D ATOM 7393 CE LYS D 478 136.120 15.312 27.725 1.00 31.88 D ATOM 7394 NZ LYS D 478 135.743 13.871 27.552 1.00 32.71 D ATOM 7395 C LYS D 478 140.218 17.984 31.402 1.00 36.46 D ATOM 7396 O LYS D 478 141.381 18.009 31.015 1.00 36.77 D ATOM 7397 N TYR D 479 139.884 17.749 32.666 1.00 35.14 D ATOM 7398 CA TYR D 479 140.906 17.514 33.675 1.00 34.37 D ATOM 7399 CB TYR D 479 140.674 18.442 34.875 1.00 33.93 D ATOM 7400 CG TYR D 479 140.847 19.914 34.543 1.00 34.98 D ATOM 7401 CD1 TYR D 479 142.108 20.529 34.614 1.00 33.05 D ATOM 7402 CE1 TYR D 479 142.264 21.880 34.300 1.00 32.76 D ATOM 7403 CD2 TYR D 479 139.753 20.691 34.147 1.00 33.92 D ATOM 7404 CE2 TYR D 479 139.901 22.037 33.830 1.00 34.11 D ATOM 7405 CZ TYR D 479 141.152 22.624 33.907 1.00 34.22 D ATOM 7406 OH TYR D 479 141.270 23.952 33.573 1.00 37.80 D ATOM 7407 C TYR D 479 140.936 16.061 34.134 1.00 32.92 D ATOM 7408 O TYR D 479 139.903 15.404 34.218 1.00 32.94 D ATOM 7409 N ILE D 480 142.138 15.569 34.412 1.00 31.23 D ATOM 7410 CA ILE D 480 142.344 14.213 34.910 1.00 30.00 D ATOM 7411 CB ILE D 480 143.568 13.528 34.236 1.00 30.27 D ATOM 7412 CG2 ILE D 480 143.826 12.150 34.879 1.00 31.07 D ATOM 7413 CG1 ILE D 480 143.335 13.334 32.741 1.00 31.12 D ATOM 7414 CD1 ILE D 480 144.440 12.531 32.060 1.00 26.66 D ATOM 7415 C ILE D 480 142.674 14.314 36.417 1.00 29.96 D ATOM 7416 O ILE D 480 143.583 15.063 36.808 1.00 29.34 D ATOM 7417 N VAL D 481 141.944 13.582 37.263 1.00 28.07 D ATOM 7418 CA VAL D 481 142.234 13.590 38.702 1.00 26.17 D ATOM 7419 CB VAL D 481 141.048 14.099 39.550 1.00 25.50 D ATOM 7420 CG1 VAL D 481 141.533 14.438 40.943 1.00 25.80 D ATOM 7421 CG2 VAL D 481 140.431 15.338 38.910 1.00 26.04 D ATOM 7422 C VAL D 481 142.587 12.166 39.110 1.00 26.07 D ATOM 7423 O VAL D 481 141.848 11.232 38.812 1.00 26.50 D ATOM 7424 N THR D 482 143.734 12.006 39.766 1.00 26.06 D ATOM 7425 CA THR D 482 144.217 10.691 40.184 1.00 26.60 D ATOM 7426 CB THR D 482 145.520 10.324 39.440 1.00 25.75 D ATOM 7427 OG1 THR D 482 146.452 11.402 39.568 1.00 23.78 D ATOM 7428 CG2 THR D 482 145.252 10.057 37.971 1.00 26.32 D ATOM 7429 C THR D 482 144.496 10.591 41.688 1.00 27.46 D ATOM 7430 O THR D 482 145.180 11.444 42.267 1.00 29.29 D ATOM 7431 N GLY D 483 143.977 9.530 42.303 1.00 25.97 D ATOM 7432 CA GLY D 483 144.176 9.303 43.724 1.00 24.32 D ATOM 7433 C GLY D 483 145.201 8.206 43.922 1.00 23.49 D ATOM 7434 O GLY D 483 145.156 7.171 43.236 1.00 23.98 D ATOM 7435 N SER D 484 146.106 8.428 44.877 1.00 22.04 D ATOM 7436 CA SER D 484 147.208 7.503 45.153 1.00 21.89 D ATOM 7437 CB SER D 484 148.540 8.193 44.820 1.00 19.14 D ATOM 7438 OG SER D 484 149.640 7.324 45.038 1.00 17.25 D ATOM 7439 C SER D 484 147.266 7.012 46.582 1.00 22.62 D ATOM 7440 O SER D 484 146.488 7.433 47.426 1.00 25.82 D ATOM 7441 N ARG D 485 148.193 6.100 46.837 1.00 24.32 D ATOM 7442 CA ARG D 485 148.412 5.585 48.179 1.00 26.12 D ATOM 7443 CB ARG D 485 149.052 4.206 48.134 1.00 27.36 D ATOM 7444 CG ARG D 485 148.168 3.160 47.556 1.00 28.76 D ATOM 7445 CD ARG D 485 148.786 1.809 47.722 1.00 29.11 D ATOM 7446 NE ARG D 485 147.768 0.784 47.543 1.00 31.30 D ATOM 7447 CZ ARG D 485 148.031 −0.500 47.350 1.00 31.33 D ATOM 7448 NH1 ARG D 485 149.283 −0.931 47.304 1.00 30.94 D ATOM 7449 NH2 ARG D 485 147.039 −1.353 47.214 1.00 31.96 D ATOM 7450 C ARG D 485 149.367 6.534 48.886 1.00 27.46 D ATOM 7451 O ARG D 485 149.712 6.329 50.045 1.00 28.74 D ATOM 7452 N ASP D 486 149.822 7.561 48.186 1.00 27.88 D ATOM 7453 CA ASP D 486 150.722 8.487 48.819 1.00 27.38 D ATOM 7454 CB ASP D 486 151.631 9.137 47.789 1.00 29.39 D ATOM 7455 CG ASP D 486 150.858 9.822 46.695 1.00 30.30 D ATOM 7456 OD1 ASP D 486 149.693 10.190 46.951 1.00 28.83 D ATOM 7457 OD2 ASP D 486 151.410 10.006 45.591 1.00 33.15 D ATOM 7458 C ASP D 486 149.947 9.547 49.566 1.00 26.08 D ATOM 7459 O ASP D 486 150.524 10.533 49.997 1.00 26.51 D ATOM 7460 N ASN D 487 148.643 9.343 49.727 1.00 26.47 D ATOM 7461 CA ASN D 487 147.778 10.295 50.449 1.00 28.03 D ATOM 7462 CB ASN D 487 148.466 10.859 51.720 1.00 24.22 D ATOM 7463 CG ASN D 487 149.130 9.783 52.608 1.00 25.85 D ATOM 7464 OD1 ASN D 487 150.077 10.094 53.357 1.00 25.75 D ATOM 7465 ND2 ASN D 487 148.639 8.536 52.543 1.00 23.88 D ATOM 7466 C ASN D 487 147.331 11.492 49.578 1.00 29.17 D ATOM 7467 O ASN D 487 146.419 12.233 49.958 1.00 30.88 D ATOM 7468 N THR D 488 147.959 11.686 48.419 1.00 30.51 D ATOM 7469 CA THR D 488 147.599 12.817 47.574 1.00 31.76 D ATOM 7470 CB THR D 488 148.867 13.590 47.044 1.00 32.19 D ATOM 7471 OG1 THR D 488 149.361 12.984 45.841 1.00 30.87 D ATOM 7472 CG2 THR D 488 149.968 13.586 48.078 1.00 32.86 D ATOM 7473 C THR D 488 146.708 12.444 46.387 1.00 33.20 D ATOM 7474 O THR D 488 146.374 11.267 46.172 1.00 32.98 D ATOM 7475 N LEU D 489 146.310 13.480 45.650 1.00 34.03 D ATOM 7476 CA LEU D 489 145.468 13.377 44.465 1.00 34.19 D ATOM 7477 CS LEU D 489 144.056 13.869 44.779 1.00 34.15 D ATOM 7478 CG LEU D 489 143.138 12.961 45.589 1.00 34.12 D ATOM 7479 CD1 LEU D 489 142.459 13.747 46.710 1.00 33.50 D ATOM 7480 CD2 LEU D 489 142.102 12.369 44.642 1.00 32.16 D ATOM 7481 C LEU D 489 146.084 14.320 43.448 1.00 33.40 D ATOM 7482 O LEU D 489 145.854 15.519 43.533 1.00 34.39 D ATOM 7483 N HIS D 490 146.876 13.818 42.506 1.00 32.48 D ATOM 7484 CA HIS D 490 147.465 14.727 41.522 1.00 31.60 D ATOM 7485 CB HIS D 490 148.744 14.136 40.909 1.00 31.07 D ATOM 7486 CG HIS D 490 149.914 14.125 41.846 1.00 31.65 D ATOM 7487 CD2 HIS D 490 149.977 14.042 43.197 1.00 32.29 D ATOM 7488 ND1 HIS D 490 151.219 14.191 41.407 1.00 33.73 D ATOM 7489 CE1 HIS D 490 152.036 14.152 42.446 1.00 33.37 D ATOM 7490 NE2 HIS D 490 151.306 14.061 43.543 1.00 32.68 D ATOM 7491 C HIS D 490 146.456 15.034 40.429 1.00 30.39 D ATOM 7492 O HIS D 490 145.735 14.149 39.983 1.00 31.27 D ATOM 7493 N VAL D 491 146.391 16.296 40.022 1.00 29.80 D ATOM 7494 CA VAL D 491 145.466 16.726 38.977 1.00 31.12 D ATOM 7495 CB VAL D 491 144.610 17.941 39.472 1.00 30.67 D ATOM 7496 CG1 VAL D 491 143.683 18.442 38.365 1.00 29.26 D ATOM 7497 CG2 VAL D 491 143.798 17.544 40.683 1.00 29.19 D ATOM 7498 C VAL D 491 146.256 17.127 37.712 1.00 32.27 D ATOM 7499 O VAL D 491 147.249 17.850 37.802 1.00 33.21 D ATOM 7500 N TRP D 492 145.829 16.647 36.545 1.00 32.46 D ATOM 7501 CA TRP D 492 146.501 16.975 35.285 1.00 33.55 D ATOM 7502 CB TRP D 492 147.308 15.798 34.759 1.00 33.18 D ATOM 7503 CG TRP D 492 147.697 14.828 35.788 1.00 34.51 D ATOM 7504 CD2 TRP D 492 149.014 14.604 36.288 1.00 35.06 D ATOM 7505 CE2 TRP D 492 148.930 13.552 37.224 1.00 34.88 D ATOM 7506 CE3 TRP D 492 150.263 15.189 36.034 1.00 33.09 D ATOM 7507 CD1 TRP D 492 146.884 13.936 36.423 1.00 34.18 D ATOM 7508 NE1 TRP D 492 147.617 13.161 37.285 1.00 34.58 D ATOM 7509 CZ2 TRP D 492 150.048 13.073 37.906 1.00 34.36 D ATOM 7510 CZ3 TRP D 492 151.371 14.715 36.710 1.00 32.50 D ATOM 7511 CH2 TRP D 492 151.258 13.667 37.634 1.00 33.38 D ATOM 7512 C TRP D 492 145.475 17.318 34.226 1.00 34.32 D ATOM 7513 O TRP D 492 144.338 16.864 34.292 1.00 35.53 D ATOM 7514 N LYS D 493 145.859 18.110 33.236 1.00 34.28 D ATOM 7515 CA LYS D 493 144.900 18.433 32.202 1.00 35.06 D ATOM 7516 CB LYS D 493 145.116 19.860 31.694 1.00 35.38 D ATOM 7517 CG LYS D 493 146.531 20.133 31.281 1.00 37.78 D ATOM 7518 CD LYS D 493 146.739 21.563 30.810 1.00 39.13 D ATOM 7519 CE LYS D 493 146.643 22.588 31.928 1.00 37.56 D ATOM 7520 NZ LYS D 493 147.094 23.906 31.410 1.00 35.80 D ATOM 7521 C LYS D 493 145.075 17.408 31.084 1.00 34.97 D ATOM 7522 O LYS D 493 146.182 17.192 30.600 1.00 33.77 D ATOM 7523 N LEU D 494 143.981 16.753 30.706 1.00 36.70 D ATOM 7524 CA LEU D 494 144.018 15.744 29.659 1.00 39.45 D ATOM 7525 CB LEU D 494 142.630 15.126 29.458 1.00 39.18 D ATOM 7526 CG LEU D 494 142.458 14.046 28.380 1.00 38.09 D ATOM 7527 CD1 LEU D 494 143.506 12.972 28.552 1.00 36.77 D ATOM 7528 CD2 LEU D 494 141.043 13.442 28.448 1.00 36.96 D ATOM 7529 C LEU D 494 144.493 16.382 28.366 1.00 42.52 D ATOM 7530 O LEU D 494 143.928 17.387 27.912 1.00 42.98 D ATOM 7531 N PRO D 495 145.559 15.819 27.764 1.00 45.09 D ATOM 7532 CD PRO D 495 146.315 14.686 28.330 1.00 45.01 D ATOM 7533 CA PRO D 495 146.168 16.287 26.505 1.00 45.59 D ATOM 7534 CB PRO D 495 147.255 15.253 26.241 1.00 45.10 D ATOM 7535 CG PRO D 495 147.633 14.802 27.619 1.00 45.87 D ATOM 7536 C PRO D 495 145.146 16.324 25.365 1.00 46.50 D ATOM 7537 O PRO D 495 144.334 15.409 25.243 1.00 47.18 D ATOM 7538 N LYS D 496 145.194 17.360 24.525 1.00 47.14 D ATOM 7539 CA LYS D 496 144.254 17.491 23.400 1.00 47.35 D ATOM 7540 CB LYS D 496 143.768 18.942 23.268 1.00 47.30 D ATOM 7541 CG LYS D 496 143.109 19.501 24.520 0.00 47.88 D ATOM 7542 CD LYS D 496 141.811 18.778 24.840 0.00 48.23 D ATOM 7543 CE LYS D 496 141.133 19.370 26.065 0.00 48.50 D ATOM 7544 NZ LYS D 496 139.817 18.722 26.331 0.00 48.74 D ATOM 7545 C LYS D 496 144.853 17.046 22.064 1.00 47.41 D ATOM 7546 O LYS D 496 145.277 15.898 21.895 1.00 46.92 D ATOM 7547 N ASP D 508 157.546 8.144 18.136 1.00 82.08 D ATOM 7548 CA ASP D 508 158.190 8.937 19.182 1.00 81.66 D ATOM 7549 CB ASP D 508 158.981 10.090 18.569 1.00 82.86 D ATOM 7550 CG ASP D 508 158.086 11.249 18.168 1.00 83.90 D ATOM 7551 OD1 ASP D 508 157.135 11.025 17.381 1.00 83.92 D ATOM 7552 OD2 ASP D 508 158.334 12.378 18.644 1.00 83.63 D ATOM 7553 C ASP D 508 157.121 9.528 20.096 1.00 80.44 D ATOM 7554 O ASP D 508 157.419 10.346 20.972 1.00 80.05 D ATOM 7555 N TYR D 509 155.874 9.120 19.884 1.00 78.72 D ATOM 7556 CA TYR D 509 154.768 9.631 20.678 1.00 76.03 D ATOM 7557 CB TYR D 509 153.454 8.997 20.254 1.00 76.05 D ATOM 7558 CG TYR D 509 152.443 10.025 19.841 1.00 77.13 D ATOM 7559 CD1 TYR D 509 152.268 11.195 20.579 1.00 77.84 D ATOM 7560 CE1 TYR D 509 151.324 12.147 20.205 1.00 79.73 D ATOM 7561 CD2 TYR D 509 151.653 9.830 18.719 1.00 78.10 D ATOM 7562 CE2 TYR D 509 150.709 10.769 18.335 1.00 79.97 D ATOM 7563 CZ TYR D 509 150.543 11.923 19.080 1.00 80.67 D ATOM 7564 OH TYR D 509 149.570 12.832 18.715 1.00 82.17 D ATOM 7565 C TYR D 509 154.938 9.440 22.170 1.00 73.80 D ATOM 7566 O TYR D 509 154.457 10.253 22.960 1.00 75.57 D ATOM 7567 N PRO D 510 155.602 8.352 22.588 1.00 70.29 D ATOM 7568 CD PRO D 510 156.084 7.160 21.860 1.00 68.38 D ATOM 7569 CA PRO D 510 155.758 8.194 24.039 1.00 66.01 D ATOM 7570 CB PRO D 510 156.600 6.929 24.150 1.00 66.48 D ATOM 7571 CG PRO D 510 156.132 6.128 22.949 1.00 68.27 D ATOM 7572 C PRO D 510 156.446 9.424 24.644 1.00 62.34 D ATOM 7573 O PRO D 510 157.667 9.504 24.676 1.00 62.17 D ATOM 7574 N LEU D 511 155.655 10.392 25.096 1.00 58.50 D ATOM 7575 CA LEU D 511 156.197 11.603 25.700 1.00 54.92 D ATOM 7576 CB LEU D 511 155.354 12.806 25.313 1.00 54.10 D ATOM 7577 CG LEU D 511 155.130 12.940 23.807 1.00 52.83 D ATOM 7578 CD1 LEU D 511 154.228 14.114 23.521 1.00 51.33 D ATOM 7579 CD2 LEU D 511 156.467 13.102 23.107 1.00 52.54 D ATOM 7580 C LEU D 511 156.188 11.451 27.211 1.00 53.49 D ATOM 7581 O LEU D 511 155.145 11.576 27.847 1.00 53.00 D ATOM 7582 N VAL D 512 157.359 11.184 27.778 1.00 52.14 D ATOM 7583 CA VAL D 512 157.506 10.992 29.213 1.00 49.88 D ATOM 7584 CB VAL D 512 158.576 9.937 29.498 1.00 48.71 D ATOM 7585 CG1 VAL D 512 158.654 9.664 30.992 1.00 49.81 D ATOM 7586 CG2 VAL D 512 158.262 8.666 28.725 1.00 47.64 D ATOM 7587 C VAL D 512 157.889 12.265 29.954 1.00 49.28 D ATOM 7588 O VAL D 512 158.855 12.925 29.592 1.00 48.19 D ATOM 7589 N PHE D 513 157.126 12.598 30.994 1.00 50.24 D ATOM 7590 CA PHE D 513 157.397 13.778 31.823 1.00 51.82 D ATOM 7591 CB PHE D 513 156.158 14.671 31.950 1.00 51.83 D ATOM 7592 CG PHE D 513 155.565 15.091 30.632 1.00 52.04 D ATOM 7593 CD1 PHE D 513 154.849 14.187 29.856 1.00 52.52 D ATOM 7594 CD2 PHE D 513 155.724 16.392 30.164 1.00 51.87 D ATOM 7595 CE1 PHE D 513 154.305 14.571 28.635 1.00 52.41 D ATOM 7596 CE2 PHE D 513 155.182 16.785 28.944 1.00 51.44 D ATOM 7597 CZ PHE D 513 154.472 15.873 28.181 1.00 51.72 D ATOM 7598 C PHE D 513 157.807 13.318 33.225 1.00 52.58 D ATOM 7599 O PHE D 513 156.957 13.164 34.100 1.00 53.73 D ATOM 7600 N HIS D 514 159.107 13.108 33.427 1.00 52.88 D ATOM 7601 CA HIS D 514 159.649 12.656 34.707 1.00 52.63 D ATOM 7602 CB HIS D 514 161.150 12.425 34.577 1.00 52.45 D ATOM 7603 CG HIS D 514 161.495 11.297 33.662 1.00 53.43 D ATOM 7604 CD2 HIS D 514 161.857 11.285 32.358 1.00 53.76 D ATOM 7605 ND1 HIS D 514 161.411 9.977 34.049 1.00 54.13 D ATOM 7606 CE1 HIS D 514 161.705 9.199 33.023 1.00 54.22 D ATOM 7607 NE2 HIS D 514 161.979 9.968 31.985 1.00 55.05 D ATOM 7608 C HIS D 514 159.388 13.615 35.855 1.00 53.18 D ATOM 7609 O HIS D 514 159.096 13.204 36.986 1.00 54.06 D ATOM 7610 N THR D 515 159.494 14.901 35.569 1.00 52.64 D ATOM 7611 CA THR D 515 159.281 15.888 36.597 1.00 52.40 D ATOM 7612 CB THR D 515 160.524 16.788 36.742 1.00 52.48 D ATOM 7613 OG1 THR D 515 160.166 17.996 37.420 1.00 52.59 D ATOM 7614 CG2 THR D 515 161.126 17.093 35.381 1.00 52.87 D ATOM 7615 C THR D 515 158.029 16.705 36.322 1.00 52.17 D ATOM 7616 O THR D 515 157.858 17.269 35.245 1.00 51.18 D ATOM 7617 N PRO D 516 157.114 16.736 37.304 1.00 53.39 D ATOM 7618 CD PRO D 516 157.164 15.841 38.478 1.00 53.89 D ATOM 7619 CA PRO D 516 155.835 17.449 37.271 1.00 52.84 D ATOM 7620 CB PRO D 516 155.231 17.119 38.632 1.00 52.59 D ATOM 7621 CG PRO D 516 155.703 15.729 38.851 1.00 52.83 D ATOM 7622 C PRO D 516 155.976 18.939 37.057 1.00 51.67 D ATOM 7623 O PRO D 516 155.238 19.533 36.279 1.00 52.06 D ATOM 7624 N GLU D 517 156.925 19.545 37.751 1.00 51.53 D ATOM 7625 CA GLD D 517 157.115 20.974 37.615 1.00 51.30 D ATOM 7626 CB GLU D 517 158.171 21.456 38.611 1.00 53.01 D ATOM 7627 CG GLU D 517 157.783 21.225 40.076 1.00 55.65 D ATOM 7628 CD GLU D 517 156.339 21.648 40.384 1.00 57.61 D ATOM 7629 OE1 GLU D 517 155.899 22.718 39.901 1.00 58.27 D ATOM 7630 OE2 GLU D 517 155.641 20.911 41.115 1.00 58.41 D ATOM 7631 C GLU D 517 157.482 21.376 36.180 1.00 50.73 D ATOM 7632 O GLD D 517 157.417 22.549 35.824 1.00 50.38 D ATOM 7633 N GLU D 518 157.853 20.408 35.350 1.00 49.94 D ATOM 7634 CA GLU D 518 158.200 20.707 33.964 1.00 48.95 D ATOM 7635 CB GLU D 518 159.552 20.081 33.613 1.00 49.87 D ATOM 7636 CG GLU D 518 160.741 20.801 34.239 1.00 51.31 D ATOM 7637 CD GLU D 518 162.074 20.125 33.945 1.00 52.52 D ATOM 7638 OE1 GLU D 518 162.225 19.579 32.823 1.00 53.98 D ATOM 7639 OE2 GLU D 518 162.971 20.153 34.826 1.00 50.01 D ATOM 7640 C GLU D 518 157.119 20.209 33.003 1.00 47.92 D ATOM 7641 O GLU D 518 157.143 20.496 31.808 1.00 47.01 D ATOM 7642 N ASN D 519 156.164 19.465 33.541 1.00 47.59 D ATOM 7643 CA ASN D 519 155.071 18.933 32.746 1.00 46.99 D ATOM 7644 CB ASN D 519 154.490 17.710 33.459 1.00 45.93 D ATOM 7645 CG ASN D 519 153.454 16.995 32.633 1.00 45.28 D ATOM 7646 OD1 ASN D 519 152.907 15.970 33.055 1.00 45.38 D ATOM 7647 ND2 ASN D 519 153.173 17.526 31.445 1.00 42.56 D ATOM 7648 C ASN D 519 153.998 20.023 32.551 1.00 46.69 D ATOM 7649 O ASN D 519 153.408 20.516 33.524 1.00 46.92 D ATOM 7650 N PRO D 520 153.758 20.431 31.291 1.00 45.28 D ATOM 7651 CD PRO D 520 154.544 20.037 30.110 1.00 43.44 D ATOM 7652 CA PRO D 520 152.769 21.460 30.937 1.00 44.93 D ATOM 7653 CB PRO D 520 152.965 21.621 29.431 1.00 43.10 D ATOM 7654 CG PRO D 520 154.396 21.232 29.234 1.00 43.83 D ATOM 7655 C PRO D 520 151.328 21.058 31.265 1.00 44.42 D ATOM 7656 O PRO D 520 150.430 21.899 31.341 1.00 45.05 D ATOM 7657 N TYR D 521 151.126 19.764 31.465 1.00 43.22 D ATOM 7658 CA TYR D 521 149.808 19.216 31.733 1.00 42.86 D ATOM 7659 CB TYR D 521 149.707 17.885 31.017 1.00 42.46 D ATOM 7660 CG TYR D 521 150.006 17.994 29.543 1.00 41.84 D ATOM 7661 CD1 TYR D 521 149.117 18.639 28.684 1.00 43.00 D ATOM 7662 CE1 TYR D 521 149.330 18.673 27.315 1.00 42.26 D ATOM 7663 CD2 TYR D 521 151.135 17.395 28.996 1.00 42.03 D ATOM 7664 CE2 TYR D 521 151.363 17.422 27.625 1.00 42.28 D ATOM 7665 CZ TYR D 521 150.445 18.058 26.788 1.00 43.30 D ATOM 7666 OH TYR D 521 150.592 18.015 25.418 1.00 44.00 D ATOM 7667 C TYR D 521 149.444 19.047 33.211 1.00 42.72 D ATOM 7668 O TYR D 521 148.267 18.922 33.567 1.00 42.06 D ATOM 7669 N PHE D 522 150.459 19.030 34.065 1.00 41.61 D ATOM 7670 CA PHE D 522 150.263 18.902 35.500 1.00 40.23 D ATOM 7671 CB PHE D 522 151.606 18.630 36.163 1.00 40.93 D ATOM 7672 CG PHE D 522 151.580 18.761 37.646 1.00 41.77 D ATOM 7673 CD1 PHE D 522 150.784 17.923 38.415 1.00 42.70 D ATOM 7674 CD2 PHE D 522 152.362 19.716 38.280 1.00 42.48 D ATOM 7675 CE1 PHE D 522 150.770 18.030 39.800 1.00 43.11 D ATOM 7676 CE2 PHE D 522 152.357 19.835 39.665 1.00 43.56 D ATOM 7677 CZ PHE D 522 151.559 18.989 40.427 1.00 44.10 D ATOM 7678 C PHE D 522 149.682 20.218 36.013 1.00 38.95 D ATOM 7679 O PHE D 522 149.994 21.271 35.470 1.00 38.64 D ATOM 7680 N VAL D 523 148.823 20.169 37.028 1.00 38.34 D ATOM 7681 CA VAL D 523 148.256 21.407 37.559 1.00 38.44 D ATOM 7682 CB VAL D 523 146.720 21.500 37.351 1.00 37.33 D ATOM 7683 CG1 VAL D 523 146.352 21.189 35.900 1.00 35.81 D ATOM 7684 CG2 VAL D 523 146.020 20.585 38.298 1.00 39.53 D ATOM 7685 C VAL D 523 148.543 21.590 39.044 1.00 38.09 D ATOM 7686 O VAL D 523 148.774 22.712 39.510 1.00 38.38 D ATOM 7687 N GLY D 524 148.543 20.484 39.780 1.00 36.48 D ATOM 7688 CA GLY D 524 148.798 20.567 41.203 1.00 35.67 D ATOM 7689 C GLY D 524 148.389 19.349 42.012 1.00 34.74 D ATOM 7690 O GLY D 524 147.705 18.446 41.512 1.00 36.14 D ATOM 7691 N VAL D 525 148.812 19.351 43.276 1.00 32.26 D ATOM 7692 CA VAL D 525 148.563 18.270 44.224 1.00 28.84 D ATOM 7693 CB VAL D 525 149.834 17.940 44.980 1.00 28.68 D ATOM 7694 CG1 VAL D 525 149.536 16.914 46.060 1.00 28.23 D ATOM 7695 CG2 VAL D 525 150.913 17.467 43.993 1.00 27.71 D ATOM 7696 C VAL D 525 147.522 18.613 45.261 1.00 27.86 D ATOM 7697 O VAL D 525 147.686 19.580 45.985 1.00 29.26 D ATOM 7698 N LEU D 526 146.469 17.807 45.349 1.00 26.79 D ATOM 7699 CA LEU D 526 145.421 18.028 46.341 1.00 24.97 D ATOM 7700 CB LEU D 526 144.082 17.539 45.796 1.00 24.09 D ATOM 7701 CG LEU D 526 143.105 18.496 45.072 1.00 25.53 D ATOM 7702 CD1 LEU D 526 143.706 19.861 44.714 1.00 21.96 D ATOM 7703 CD2 LEU D 526 142.600 17.770 43.842 1.00 24.82 D ATOM 7704 C LEU D 526 145.771 17.305 47.659 1.00 25.98 D ATOM 7705 O LEU D 526 145.389 16.153 47.865 1.00 26.01 D ATOM 7706 N ARG D 527 146.507 18.008 48.533 1.00 26.45 D ATOM 7707 CA ARG D 527 146.953 17.504 49.839 1.00 27.15 D ATOM 7708 CB ARG D 527 148.068 18.359 50.423 1.00 29.53 D ATOM 7709 CG ARG D 527 149.136 18.793 49.481 1.00 30.78 D ATOM 7710 CD ARG D 527 150.199 17.750 49.353 1.00 29.79 D ATOM 7711 NE ARG D 527 151.289 18.254 48.534 1.00 28.82 D ATOM 7712 CZ ARG D 527 152.426 17.609 48.341 1.00 28.06 D ATOM 7713 NH1 ARG D 527 152.621 16.424 48.913 1.00 27.74 D ATOM 7714 NH2 ARG D 527 153.361 18.156 47.578 1.00 28.96 D ATOM 7715 C ARG D 527 145.833 17.583 50.854 1.00 27.48 D ATOM 7716 O ARG D 527 145.198 18.625 50.982 1.00 28.10 D ATOM 7717 N GLY D 528 145.643 16.511 51.618 1.00 27.13 D ATOM 7718 CA GLY D 528 144.593 16.502 52.618 1.00 25.97 D ATOM 7719 C GLY D 528 144.378 15.186 53.350 1.00 27.12 D ATOM 7720 O GLY D 528 144.222 15.170 54.573 1.00 26.85 D ATOM 7721 N HIS D 529 144.349 14.076 52.619 1.00 28.35 D ATOM 7722 CA HIS D 529 144.148 12.771 53.242 1.00 28.78 D ATOM 7723 CB HIS D 529 143.686 11.747 52.197 1.00 29.36 D ATOM 7724 CG HIS D 529 142.272 11.942 51.729 1.00 31.01 D ATOM 7725 CD2 HIS D 529 141.776 12.234 50.502 1.00 32.50 D ATOM 7726 ND1 HIS D 529 141.181 11.808 52.562 1.00 29.94 D ATOM 7727 CE1 HIS D 529 140.074 12.010 51.864 1.00 32.77 D ATOM 7728 NE2 HIS D 529 140.409 12.270 50.613 1.00 31.73 D ATOM 7729 C HIS D 529 145.428 12.293 53.922 1.00 29.06 D ATOM 7730 O HIS D 529 146.525 12.716 53.562 1.00 29.97 D ATOM 7731 N MSE D 530 145.278 11.412 54.906 1.00 30.41 D ATOM 7732 CA MSE D 530 146.411 10.872 55.662 1.00 31.44 D ATOM 7733 CB MSE D 530 146.116 10.979 57.163 1.00 36.54 D ATOM 7734 CG MSE D 530 145.727 12.383 57.647 1.00 40.77 D ATOM 7735 SE MSE D 530 147.225 13.555 57.992 1.00 48.72 D ATOM 7736 CE MSE D 530 147.747 12.886 59.726 1.00 44.45 D ATOM 7737 C MSE D 530 146.708 9.409 55.286 1.00 30.15 D ATOM 7738 O MSE D 530 147.663 8.804 55.770 1.00 31.06 D ATOM 7739 N ALA D 531 145.872 8.837 54.433 1.00 27.91 D ATOM 7740 CA ALA D 531 146.077 7.470 53.983 1.00 25.52 D ATOM 7741 CB ALA D 531 145.322 6.506 54.863 1.00 23.17 D ATOM 7742 C ALA D 531 145.634 7.329 52.528 1.00 25.05 D ATOM 7743 O ALA D 531 145.166 8.283 51.903 1.00 25.19 D ATOM 7744 N SER D 532 145.778 6.126 52.004 1.00 24.01 D ATOM 7745 CA SER D 532 145.431 5.834 50.635 1.00 23.62 D ATOM 7746 CB SER D 532 145.452 4.332 50.427 1.00 23.66 D ATOM 7747 OG SER D 532 145.044 4.009 49.120 1.00 24.72 D ATOM 7748 C SER D 532 144.093 6.391 50.161 1.00 24.24 D ATOM 7749 O SER D 532 143.059 6.249 50.835 1.00 23.67 D ATOM 7750 N VAL D 533 144.131 7.028 48.987 1.00 22.26 D ATOM 7751 CA VAL D 533 142.930 7.588 48.383 1.00 21.80 D ATOM 7752 CB VAL D 533 143.238 8.790 47.509 1.00 19.37 D ATOM 7753 CG1 VAL D 533 141.973 9.225 46.786 1.00 19.14 D ATOM 7754 CG2 VAL D 533 143.757 9.912 48.367 1.00 16.33 D ATOM 7755 C VAL D 533 142.311 6.476 47.564 1.00 23.09 D ATOM 7756 O VAL D 533 142.740 6.181 46.464 1.00 24.67 D ATOM 7757 N ARG D 534 141.281 5.865 48.125 1.00 23.37 D ATOM 7758 CA ARG D 534 140.630 4.734 47.514 1.00 21.94 D ATOM 7759 CB ARG D 534 139.887 3.966 48.588 1.00 22.94 D ATOM 7760 CG ARG D 534 139.334 2.660 48.104 1.00 20.89 D ATOM 7761 CD ARG D 534 140.460 1.735 47.688 1.00 20.13 D ATOM 7762 NE ARG D 534 139.934 0.404 47.470 1.00 22.05 D ATOM 7763 CZ ARG D 534 139.177 0.061 46.435 1.00 21.88 D ATOM 7764 NH1 ARG D 534 138.859 0.955 45.499 1.00 16.38 D ATOM 7765 NH2 ARG D 534 138.723 −1.184 46.354 1.00 21.24 D ATOM 7766 C ARG D 534 139.687 4.934 46.350 1.00 21.77 D ATOM 7767 O ARG D 534 139.630 4.082 45.464 1.00 23.87 D ATOM 7768 N THR 0535 138.944 6.029 46.328 1.00 21.46 D ATOM 7769 CA THR D 535 137.976 6.186 45.252 1.00 23.21 D ATOM 7770 CB THR D 535 136.630 5.607 45.693 1.00 22.72 D ATOM 7771 OG1 THR D 535 135.615 5.908 44.728 1.00 24.25 D ATOM 7772 CG2 THR D 535 136.255 6.189 47.038 1.00 21.59 D ATOM 7773 C THR D 535 137.785 7.623 44.871 1.00 22.36 D ATOM 7774 O THR D 535 138.010 8.494 45.692 1.00 22.27 D ATOM 7775 N VAL D 536 137.383 7.869 43.627 1.00 23.47 D ATOM 7776 CA VAL D 536 137.154 9.240 43.178 1.00 26.56 D ATOM 7777 CB VAL D 536 138.340 9.805 42.381 1.00 27.30 D ATOM 7778 CG1 VAL D 536 138.152 11.303 42.178 1.00 27.76 D ATOM 7779 CG2 VAL D 536 139.615 9.573 43.126 1.00 29.04 D ATOM 7780 C VAL D 536 135.907 9.379 42.330 1.00 26.74 D ATOM 7781 O VAL D 536 135.550 8.486 41.558 1.00 28.31 D ATOM 7782 N SER D 537 135.248 10.517 42.473 1.00 26.29 D ATOM 7783 CA SER D 537 134.019 10.759 41.741 1.00 25.58 D ATOM 7784 CB SER D 537 132.832 10.197 42.529 1.00 23.69 D ATOM 7785 OC SER D 537 131.605 10.436 41.878 1.00 19.22 D ATOM 7786 C SER D 537 133.859 12.252 41.547 1.00 26.69 D ATOM 7787 O SER D 537 133.697 13.000 42.517 1.00 27.22 D ATOM 7788 N GLY D 538 133.923 12.684 40.294 1.00 26.82 D ATOM 7789 CA GLY D 538 133.794 14.096 40.020 1.00 28.64 D ATOM 7790 C GLY D 538 133.027 14.446 38.766 1.00 28.83 D ATOM 7791 O GLY D 538 132.961 13.666 37.820 1.00 29.17 D ATOM 7792 N HIS D 539 132.450 15.645 38.790 1.00 29.15 D ATOM 7793 CA HIS D 539 131.679 16.226 37.696 1.00 27.88 D ATOM 7794 CB HIS D 539 130.179 16.025 37.911 1.00 27.43 D ATOM 7795 CG HIS D 539 129.333 16.567 36.799 1.00 28.11 D ATOM 7796 CD2 HIS D 539 128.736 17.772 36.637 1.00 30.46 D ATOM 7797 ND1 HIS D 539 129.046 15.843 35.662 1.00 27.67 D ATOM 7798 CE1 HIS D 539 128.307 16.577 34.848 1.00 29.05 D ATOM 7799 NE2 HIS D 539 128.105 17.753 35.415 1.00 30.92 D ATOM 7800 C HIS D 539 131.959 17.735 37.697 1.00 29.12 D ATOM 7801 O HIS D 539 131.791 18.409 38.728 1.00 28.57 D ATOM 7802 N GLY D 540 132.376 18.261 36.546 1.00 28.54 D ATOM 7803 CA GLY D 540 132.650 19.682 36.436 1.00 27.08 D ATOM 7804 C GLY D 540 133.872 20.122 37.215 1.00 27.09 D ATOM 7805 O GLY D 540 134.904 19.454 37.179 1.00 28.54 D ATOM 7806 N ASN D 541 133.777 21.245 37.920 1.00 25.16 D ATOM 7807 CA ASN D 541 134.924 21.706 38.679 1.00 24.86 D ATOM 7808 CB ASN D 541 134.907 23.237 38.816 1.00 26.35 D ATOM 7809 CG ASN D 541 133.889 23.726 39.851 1.00 29.47 D ATOM 7810 OD1 ASN D 541 132.706 23.341 39.803 1.00 29.21 D ATOM 7811 ND2 ASN D 541 134.341 24.575 40.792 1.00 26.35 D ATOM 7812 C ASN D 541 134.915 21.062 40.056 1.00 24.63 D ATOM 7813 O ASN D 541 135.803 21.308 40.864 1.00 25.54 D ATOM 7814 N ILE D 542 133.921 20.220 40.321 1.00 22.93 D ATOM 7815 CA ILE D 542 133.821 19.574 41.629 1.00 22.46 D ATOM 7816 CB ILE D 542 132.361 19.724 42.186 1.00 20.91 D ATOM 7817 CG2 ILE D 542 132.215 18.977 43.497 1.00 22.05 D ATOM 7818 CG1 ILE D 542 132.001 21.215 42.385 1.00 19.70 D ATOM 7819 CD1 ILE D 542 132.866 22.016 43.388 1.00 10.85 D ATOM 7820 C ILE D 542 134.258 18.085 41.663 1.00 24.27 D ATOM 7821 O ILE D 542 133.841 17.258 40.832 1.00 23.68 D ATOM 7822 N VAL D 543 135.108 17.738 42.624 1.00 24.95 D ATOM 7823 CA VAL D 543 135.565 16.350 42.735 1.00 26.33 D ATOM 7824 CB VAL D 543 137.023 16.176 42.199 1.00 28.00 D ATOM 7825 CG1 VAL D 543 137.492 14.742 42.406 1.00 27.16 D ATOM 7826 CG2 VAL D 543 137.073 16.515 40.716 1.00 30.18 D ATOM 7827 C VAL D 543 135.509 15.864 44.174 1.00 25.02 D ATOM 7828 O VAL D 543 135.893 16.601 45.079 1.00 24.45 D ATOM 7829 N VAL D 544 135.017 14.639 44.388 1.00 24.93 D ATOM 7830 CA VAL D 544 134.939 14.093 45.748 1.00 25.31 D ATOM 7831 CB VAL D 544 133.495 13.783 46.197 1.00 24.60 D ATOM 7832 CG1 VAL D 544 133.507 13.509 47.679 1.00 24.71 D ATOM 7833 CG2 VAL D 544 132.553 14.940 45.889 1.00 25.25 D ATOM 7834 C VAL D 544 135.750 12.814 45.910 1.00 25.25 D ATOM 7835 O VAL D 544 135.662 11.903 45.082 1.00 26.67 D ATOM 7836 N SER D 545 136.534 12.745 46.985 1.00 24.15 D ATOM 7837 CA SER D 545 137.367 11.566 47.236 1.00 24.66 D ATOM 7838 CB SER D 545 138.835 11.960 47.213 1.00 22.85 D ATOM 7839 OG SER D 545 139.110 12.914 48.221 1.00 26.17 D ATOM 7840 C SER D 545 137.105 10.777 48.525 1.00 26.03 D ATOM 7841 O SER D 545 136.609 11.315 49.516 1.00 27.76 D ATOM 7842 N GLY D 546 137.467 9.497 48.495 1.00 25.26 D ATOM 7843 CA GLY D 546 137.292 8.642 49.647 1.00 24.44 D ATOM 7844 C GLY D 546 138.637 8.073 50.039 1.00 24.54 D ATOM 7845 O GLY D 546 139.318 7.450 49.220 1.00 23.24 D ATOM 7846 N SER D 547 139.038 8.282 51.288 1.00 25.20 D ATOM 7847 CA SER D 547 140.339 7.773 51.730 1.00 27.40 D ATOM 7848 CB SER D 547 141.235 8.897 52.239 1.00 25.06 D ATOM 7849 OG SER D 547 142.424 8.333 52.763 1.00 23.13 D ATOM 7850 C SER D 547 140.286 6.723 52.816 1.00 28.75 D ATOM 7851 O SER D 547 139.260 6.520 53.462 1.00 32.39 D ATOM 7852 N TYR D 548 141.411 6.062 53.031 1.00 27.35 D ATOM 7853 CA TYR D 548 141.457 5.071 54.078 1.00 24.34 D ATOM 7854 CB TYR D 548 142.588 4.085 53.835 1.00 21.23 D ATOM 7855 CG TYR D 548 142.185 2.933 52.964 1.00 18.24 D ATOM 7856 CD1 TYR D 548 140.975 2.940 52.267 1.00 17.37 D ATOM 7857 CE1 TYR D 548 140.631 1.894 51.426 1.00 15.22 D ATOM 7858 CD2 TYR D 548 143.030 1.850 52.802 1.00 18.07 D ATOM 7859 CE2 TYR D 548 142.701 0.796 51.969 1.00 15.33 D ATOM 7860 CZ TYR D 548 141.507 0.825 51.283 1.00 17.35 D ATOM 7861 OH TYR D 548 141.195 −0.213 50.435 1.00 18.41 D ATOM 7862 C TYR D 548 141.637 5.742 55.428 1.00 25.52 D ATOM 7863 O TYR D 548 141.897 5.060 56.401 1.00 24.80 D ATOM 7864 N ASP D 549 141.517 7.070 55.496 1.00 26.28 D ATOM 7865 CA ASP D 549 141.637 7.739 56.789 1.00 26.66 D ATOM 7866 CB ASP D 549 142.332 9.114 56.693 1.00 28.11 D ATOM 7867 CG ASP D 549 141.761 10.006 55.611 1.00 28.18 D ATOM 7868 OD1 ASP D 549 140.580 9.822 55.227 1.00 30.65 D ATOM 7869 OD2 ASP D 549 142.507 10.909 55.167 1.00 25.41 D ATOM 7870 C ASP D 549 140.239 7.884 57.363 1.00 26.46 D ATOM 7871 O ASP D 549 140.014 8.634 58.311 1.00 26.79 D ATOM 7872 N ASN D 550 139.309 7.157 56.742 1.00 26.14 D ATOM 7873 CA ASN D 550 137.906 7.115 57.139 1.00 24.53 D ATOM 7874 CB ASN D 550 137.825 6.849 58.633 1.00 23.45 D ATOM 7875 CG ASN D 550 138.484 5.542 59.012 1.00 23.88 D ATOM 7876 OD1 ASN D 550 139.126 4.894 58.190 1.00 24.66 D ATOM 7877 ND2 ASN D 550 138.319 5.143 60.253 1.00 25.10 D ATOM 7878 C ASN D 550 137.162 8.374 56.796 1.00 23.51 D ATOM 7879 O ASN D 550 136.006 8.534 57.146 1.00 23.99 D ATOM 7880 N THR D 551 137.811 9.237 56.038 1.00 24.61 D ATOM 7881 CA THR D 551 137.221 10.510 55.706 1.00 24.98 D ATOM 7882 CB THR D 551 138.155 11.584 56.208 1.00 25.84 D ATOM 7883 OG1 THR D 551 137.402 12.640 56.803 1.00 26.76 D ATOM 7884 CG2 THR D 551 139.015 12.107 55.053 1.00 24.97 D ATOM 7885 C THR D 551 136.993 10.725 54.206 1.00 25.92 D ATOM 7886 O THR D 551 137.535 9.996 53.376 1.00 24.99 D ATOM 7887 N LEU D 552 136.173 11.719 53.868 1.00 26.68 D ATOM 7888 CA LEU D 552 135.934 12.079 52.471 1.00 26.79 D ATOM 7889 CB LEU D 552 134.508 11.771 52.031 1.00 24.86 D ATOM 7890 CG LEU D 552 134.189 10.328 51.665 1.00 23.77 D ATOM 7891 CD1 LEU D 552 133.215 9.804 52.689 1.00 23.78 D ATOM 7892 CD2 LEU D 552 133.597 10.237 50.257 1.00 22.54 D ATOM 7893 C LEU D 552 136.180 13.572 52.308 1.00 27.51 D ATOM 7894 O LEU D 552 135.792 14.366 53.170 1.00 28.40 D ATOM 7895 N ILE D 553 136.828 13.955 51.206 1.00 27.13 D ATOM 7896 CA ILE D 553 137.102 15.372 50.939 1.00 25.65 D ATOM 7897 CE ILE D 553 138.623 15.686 50.957 1.00 24.82 D ATOM 7898 CG2 ILE D 553 138.854 17.153 50.606 1.00 24.33 D ATOM 7899 CG1 ILE D 553 139.212 15.444 52.355 1.00 25.26 D ATOM 7900 CD1 ILE D 553 140.725 15.613 52.413 1.00 24.18 D ATOM 7901 C ILE D 553 136.531 15.869 49.606 1.00 25.82 D ATOM 7902 O ILE D 553 136.664 15.210 48.561 1.00 24.35 D ATOM 7903 N VAL D 554 135.889 17.038 49.672 1.00 24.96 D ATOM 7904 CA VAL D 554 135.299 17.704 48.503 1.00 24.79 D ATOM 7905 CB VAL D 554 133.964 18.425 48.858 1.00 21.69 D ATOM 7906 CG1 VAL D 554 133.366 19.041 47.620 1.00 19.43 D ATOM 7907 CG2 VAL D 554 133.000 17.455 49.480 1.00 21.35 D ATOM 7908 C VAL D 554 136.308 18.753 48.016 1.00 26.46 D ATOM 7909 O VAL D 554 136.646 19.689 48.746 1.00 26.64 D ATOM 7910 N TRP D 555 136.812 18.574 46.797 1.00 27.69 D ATOM 7911 CA TRP D 555 137.784 19.500 46.233 1.00 28.09 D ATOM 7912 CB TRP D 555 139.026 18.767 45.703 1.00 28.18 D ATOM 7913 CG TRP D 555 139.593 17.681 46.576 1.00 29.63 D ATOM 7914 CD2 TRP D 555 140.695 17.795 47.487 1.00 30.60 D ATOM 7915 CE2 TRP D 555 140.948 16.505 48.003 1.00 30.79 D ATOM 7916 CE3 TRP D 555 141.492 18.862 47.915 1.00 30.24 D ATOM 7917 CD1 TRP D 555 139.228 16.365 46.587 1.00 29.55 D ATOM 7918 NE1 TRP D 555 140.041 15.652 47.436 1.00 30.90 D ATOM 7919 CZ2 TRP D 555 141.968 16.253 48.921 1.00 31.50 D ATOM 7920 CZ3 TRP D 555 142.510 18.608 48.832 1.00 31.00 D ATOM 7921 CH2 TRP D 555 142.736 17.314 49.323 1.00 31.35 D ATOM 7922 C TRP D 555 137.210 20.306 45.075 1.00 27.75 D ATOM 7923 O TRP D 555 136.392 19.807 44.297 1.00 26.08 D ATOM 7924 N ASP D 556 137.658 21.556 44.981 1.00 29.07 D ATOM 7925 CA ASP D 556 137.274 22.463 43.904 1.00 29.82 D ATOM 7926 CB ASP D 556 136.917 23.849 44.425 1.00 33.43 D ATOM 7927 CG ASP D 556 136.336 24.762 43.335 1.00 36.51 D ATOM 7928 OD1 ASP D 556 136.913 24.864 42.216 1.00 35.80 D ATOM 7929 OD2 ASP D 556 135.285 25.388 43.609 1.00 39.49 D ATOM 7930 C ASP D 556 138.539 22.591 43.095 1.00 28.83 D ATOM 7931 O ASP D 556 139.440 23.337 43.463 1.00 25.39 D ATOM 7932 N VAL D 557 138.596 21.858 41.995 1.00 31.59 D ATOM 7933 CA VAL D 557 139.756 21.853 41.123 1.00 34.16 D ATOM 7934 CE VAL D 557 139.592 20.840 40.007 1.00 34.22 D ATOM 7935 CG1 VAL D 557 140.777 20.942 39.064 1.00 36.74 D ATOM 7936 CG2 VAL D 557 139.460 19.444 40.582 1.00 31.24 D ATOM 7937 C VAL D 557 140.021 23.183 40.466 1.00 35.74 D ATOM 7938 O VAL D 557 141.168 23.535 40.244 1.00 37.94 D ATOM 7939 N ALA D 558 138.959 23.906 40.133 1.00 37.02 D ATOM 7940 CA ALA D 558 139.107 25.196 39.485 1.00 37.13 D ATOM 7941 CB ALA D 558 137.747 25.730 39.065 1.00 39.25 D ATOM 7942 C ALA D 558 139.784 26.167 40.430 1.00 36.58 D ATOM 7943 O ALA D 558 140.342 27.168 39.997 1.00 37.02 D ATOM 7944 N GLN D 559 139.729 25.857 41.722 1.00 37.85 D ATOM 7945 CA GLN D 559 140.327 26.688 42.763 1.00 37.56 D ATOM 7946 CB GLN D 559 139.248 27.110 43.750 1.00 37.90 D ATOM 7947 CG GLN D 559 139.672 28.264 44.624 1.00 43.44 D ATOM 7948 CD GLN D 559 138.523 28.874 45.444 1.00 45.28 D ATOM 7949 OE1 GLN D 559 137.375 28.927 44.987 1.00 46.49 D ATOM 7950 NE2 GLN D 559 138.839 29.354 46.655 1.00 45.82 D ATOM 7951 C GLN D 559 141.419 25.896 43.479 1.00 37.70 D ATOM 7952 O GLN D 559 142.131 26.428 44.336 1.00 36.85 D ATOM 7953 N MSE D 560 141.535 24.624 43.094 1.00 38.22 D ATOM 7954 CA MSE D 560 142.505 23.687 43.645 1.00 37.94 D ATOM 7955 CB MSE D 560 143.870 23.912 42.984 1.00 37.36 D ATOM 7956 CG MSE D 560 144.681 22.648 42.719 1.00 37.70 D ATOM 7957 SE MSE D 560 143.786 21.540 41.377 1.00 39.17 D ATOM 7958 CE MSE D 560 143.835 22.738 39.886 1.00 41.26 D ATOM 7959 C MSE D 560 142.597 23.865 45.164 1.00 37.81 D ATOM 7960 O MSE D 560 143.675 24.035 45.710 1.00 39.53 D ATOM 7961 N LYS D 561 141.449 23.844 45.832 1.00 37.74 D ATOM 7962 CA LYS D 561 141.384 23.995 47.279 1.00 38.73 D ATOM 7963 CB LYS D 561 141.037 25.452 47.638 1.00 39.81 D ATOM 7964 CG LYS D 561 142.191 26.428 47.399 0.00 40.07 D ATOM 7965 CD LYS D 561 143.372 26.124 48.318 0.00 40.65 D ATOM 7966 CE LYS D 561 142.998 26.355 49.774 0.00 41.01 D ATOM 7967 NZ LYS D 561 144.024 25.827 50.715 0.00 41.29 D ATOM 7968 C LYS D 561 140.356 23.022 47.887 1.00 39.22 D ATOM 7969 O LYS D 561 139.419 22.584 47.208 1.00 38.84 D ATOM 7970 N CYS D 562 140.556 22.670 49.159 1.00 38.90 D ATOM 7971 CA CYS D 562 139.668 21.759 49.885 1.00 38.52 D ATOM 7972 CB CYS D 562 140.360 21.270 51.164 1.00 38.67 D ATOM 7973 SG CYS D 562 139.309 20.275 52.277 1.00 44.51 D ATOM 7974 C CYS D 562 138.402 22.521 50.260 1.00 37.58 D ATOM 7975 O CYS D 562 138.494 23.572 50.888 1.00 40.09 D ATOM 7976 N LEU D 563 137.223 22.015 49.895 1.00 34.69 D ATOM 7977 CA LEU D 563 135.981 22.726 50.232 1.00 31.60 D ATOM 7978 CB LEU D 563 134.924 22.550 49.132 1.00 28.39 D ATOM 7979 CG LEU D 563 135.214 23.279 47.820 1.00 25.92 D ATOM 7980 CD1 LEU D 563 133.986 23.317 46.939 1.00 24.65 D ATOM 7981 CD2 LEU D 563 135.679 24.670 48.139 1.00 23.99 D ATOM 7982 C LEU D 563 135.388 22.281 51.552 1.00 30.82 D ATOM 7983 O LEU D 563 135.012 23.099 52.388 1.00 29.72 D ATOM 7984 N TYR D 564 135.320 20.968 51.723 1.00 31.20 D ATOM 7985 CA TYR D 564 134.768 20.358 52.915 1.00 29.79 D ATOM 7986 CB TYR D 564 133.276 20.087 52.705 1.00 31.53 D ATOM 7987 CG TYR D 564 132.415 21.316 52.480 1.00 35.18 D ATOM 7988 CD1 TYR D 564 132.216 22.250 53.503 1.00 35.47 D ATOM 7989 CE1 TYR D 564 131.381 23.356 53.321 1.00 37.11 D ATOM 7990 CD2 TYR D 564 131.757 21.522 51.257 1.00 35.79 D ATOM 7991 CE2 TYR D 564 130.918 22.626 51.064 1.00 37.32 D ATOM 7992 CZ TYR D 564 130.733 23.539 52.100 1.00 37.56 D ATOM 7993 OH TYR D 564 129.901 24.625 51.926 1.00 37.99 D ATOM 7994 C TYR D 564 135.464 19.028 53.213 1.00 28.42 D ATOM 7995 O TYR D 564 135.998 18.357 52.323 1.00 29.93 D ATOM 7996 N ILE D 565 135.448 18.655 54.482 1.00 26.22 D ATOM 7997 CA ILE D 565 136.001 17.389 54.916 1.00 24.23 D ATOM 7998 CB ILE D 565 137.222 17.574 55.861 1.00 24.90 D ATOM 7999 CG2 ILE D 565 137.641 16.232 56.471 1.00 22.64 D ATOM 8000 CG1 ILE D 565 138.389 18.173 55.066 1.00 23.83 D ATOM 8001 CD1 ILE D 565 139.596 18.476 55.898 1.00 22.10 D ATOM 8002 C ILE D 565 134.853 16.708 55.654 1.00 24.14 D ATOM 8003 O ILE D 565 134.436 17.123 56.745 1.00 24.92 D ATOM 8004 N LEU D 566 134.319 15.674 55.022 1.00 23.68 D ATOM 8005 CA LEU D 566 133.209 14.910 55.567 1.00 21.44 D ATOM 8006 CB LEU D 566 132.498 14.204 54.433 1.00 18.60 D ATOM 8007 CG LEU D 566 132.249 15.108 53.240 1.00 16.04 D ATOM 8008 CD1 LEU D 566 131.493 14.312 52.195 1.00 18.64 D ATOM 8009 CD2 LEU D 566 131.471 16.327 53.661 1.00 11.95 D ATOM 8010 C LEU D 566 133.725 13.876 56.532 1.00 20.93 D ATOM 8011 O LEU D 566 134.448 12.975 56.126 1.00 21.77 D ATOM 8012 N SER D 567 133.345 13.980 57.800 1.00 22.31 D ATOM 8013 CA SER D 567 133.806 12.995 58.783 1.00 23.94 D ATOM 8014 CB SER D 567 134.810 13.630 59.731 1.00 23.34 D ATOM 8015 OG SER D 567 135.808 14.311 58.987 1.00 24.18 D ATOM 8016 C SER D 567 132.676 12.349 59.568 1.00 24.28 D ATOM 8017 O SER D 567 131.586 12.904 59.663 1.00 24.81 D ATOM 8018 N GLY D 568 132.950 11.166 60.113 1.00 25.74 D ATOM 8019 CA GLY D 568 131.953 10.416 60.858 1.00 25.21 D ATOM 8020 C GLY D 568 132.134 8.906 60.681 1.00 26.37 D ATOM 8021 O GLY D 568 132.130 8.163 61.664 1.00 27.73 D ATOM 8022 N HIS D 569 132.288 8.440 59.437 1.00 25.07 D ATOM 8023 CA HIS D 569 132.500 7.007 59.175 1.00 23.33 D ATOM 8024 CB HIS D 569 132.949 6.749 57.730 1.00 22.22 D ATOM 8025 CG HIS D 569 131.839 6.801 56.725 1.00 21.96 D ATOM 8026 CD2 HIS D 569 131.594 7.675 55.720 1.00 21.82 D ATOM 8027 ND1 HIS D 569 130.827 5.865 56.671 1.00 20.28 D ATOM 8028 CE1 HIS D 569 130.009 6.160 55.676 1.00 20.59 D ATOM 8029 NE2 HIS D 569 130.452 7.254 55.083 1.00 20.12 D ATOM 8030 C HIS D 569 133.590 6.520 60.129 1.00 24.25 D ATOM 8031 O HIS D 569 134.625 7.176 60.291 1.00 24.38 D ATOM 8032 N THR D 570 133.357 5.371 60.759 1.00 25.24 D ATOM 8033 CA THR D 570 134.296 4.806 61.724 1.00 25.54 D ATOM 8034 CE THR D 570 133.508 4.097 62.867 1.00 26.19 D ATOM 8035 OG1 THR D 570 132.385 3.381 62.321 1.00 27.58 D ATOM 8036 CG2 THR D 570 133.008 5.120 63.869 1.00 23.79 D ATOM 8037 C THR D 570 135.355 3.864 61.114 1.00 25.50 D ATOM 8038 O THR D 570 136.225 3.349 61.812 1.00 26.67 D ATOM 8039 N ASP D 571 135.279 3.628 59.811 1.00 26.22 D ATOM 8040 CA ASP D 571 136.284 2.804 59.141 1.00 25.18 D ATOM 8041 CB ASP D 571 135.810 1.365 58.999 1.00 26.72 D ATOM 8042 CG ASP D 571 136.956 0.386 59.009 1.00 28.41 D ATOM 8043 OD1 ASP D 571 138.011 0.726 58.447 1.00 30.11 D ATOM 8044 OD2 ASP D 571 136.818 −0.715 59.575 1.00 29.31 D ATOM 8045 C ASP D 571 136.590 3.382 57.759 1.00 24.07 D ATOM 8046 O ASP D 571 135.917 4.303 57.281 1.00 22.39 D ATOM 8047 N ARG D 572 137.593 2.825 57.101 1.00 23.27 D ATOM 8048 CA ARG D 572 137.976 3.314 55.781 1.00 22.84 D ATOM 8049 CB ARG D 572 139.153 2.491 55.250 1.00 21.15 D ATOM 8050 CG ARG D 572 138.981 1.032 55.408 1.00 19.04 D ATOM 8051 CD ARG D 572 140.058 0.268 54.705 1.00 20.64 D ATOM 8052 NE ARG D 572 141.341 0.249 55.393 1.00 22.31 D ATOM 8053 CZ ARG D 572 142.293 −0.649 55.130 1.00 23.14 D ATOM 8054 NH1 ARG D 572 142.071 −1.571 54.198 1.00 17.78 D ATOM 8055 NH2 ARG D 572 143.449 −0.646 55.799 1.00 23.35 D ATOM 8056 C ARG D 572 136.820 3.300 54.789 1.00 22.51 D ATOM 8057 O ARG D 572 135.914 2.475 54.922 1.00 22.42 D ATOM 8058 N ILE D 573 136.825 4.241 53.837 1.00 23.14 D ATOM 8059 CA ILE D 573 135.779 4.301 52.809 1.00 24.51 D ATOM 8060 CB ILE D 573 135.449 5.739 52.295 1.00 27.12 D ATOM 8061 CG2 ILE D 573 134.618 5.643 51.025 0.00 26.23 D ATOM 8062 CG1 ILE D 573 134.652 6.536 53.333 1.00 26.27 D ATOM 8063 CD1 ILE D 573 135.472 7.060 54.419 1.00 25.64 D ATOM 8064 C ILE D 573 136.330 3.577 51.601 1.00 24.11 D ATOM 8065 O ILE D 573 137.517 3.724 51.270 1.00 23.80 D ATOM 8066 N TYR D 574 135.459 2.830 50.927 1.00 22.78 D ATOM 8067 CA TYR D 574 135.849 2.071 49.742 1.00 22.23 D ATOM 8068 CB TYR D 574 135.498 0.583 49.951 1.00 21.98 D ATOM 8069 CG TYR D 574 136.588 −0.242 50.619 1.00 24.35 D ATOM 8070 CD1 TYR D 574 137.503 −0.992 49.853 1.00 22.37 D ATOM 8071 CE1 TYR D 574 138.524 −1.729 50.463 1.00 23.23 D ATOM 8072 CD2 TYR D 574 136.723 −0.254 52.019 1.00 24.83 D ATOM 8073 CE2 TYR D 574 137.736 −0.982 52.641 1.00 26.35 D ATOM 8074 CZ TYR D 574 138.639 −1.719 51.862 1.00 25.64 D ATOM 8075 OH TYR D 574 139.650 −2.423 52.493 1.00 26.87 D ATOM 8076 C TYR D 574 135.245 2.570 48.402 1.00 21.18 D ATOM 8077 O TYR D 574 135.716 2.188 47.325 1.00 22.28 D ATOM 8078 N SER D 575 134.231 3.432 48.464 1.00 19.10 D ATOM 8079 CA SER D 575 133.556 3.933 47.258 1.00 18.07 D ATOM 8080 CB SER D 575 132.559 2.872 46.756 1.00 18.09 D ATOM 8081 OG SER D 575 131.552 3.435 45.926 1.00 17.37 D ATOM 8082 C SER D 575 132.814 5.255 47.504 1.00 17.95 D ATOM 8083 O SER D 575 132.312 5.515 48.599 1.00 17.19 D ATOM 8084 N THR D 576 132.731 6.105 46.498 1.00 17.64 D ATOM 8085 CA THR D 576 132.009 7.334 46.737 1.00 19.01 D ATOM 8086 CB THR D 576 132.936 8.441 47.285 1.00 17.27 D ATOM 8087 OG1 THR D 576 132.145 9.575 47.662 1.00 15.53 D ATOM 8088 CG2 THR D 576 133.968 8.869 46.228 1.00 20.28 D ATOM 8089 C THR D 576 131.369 7.808 45.454 1.00 19.84 D ATOM 8090 O THR D 576 131.878 7.565 44.358 1.00 20.54 D ATOM 8091 N ILE D 577 130.228 8.461 45.571 1.00 18.92 D ATOM 8092 CA ILE D 577 129.622 8.959 44.366 1.00 20.24 D ATOM 8093 CB ILE D 577 128.395 8.161 43.984 1.00 19.47 D ATOM 8094 CG2 ILE D 577 127.588 8.938 42.958 1.00 17.51 D ATOM 8095 CG1 ILE D 577 128.818 6.790 43.456 1.00 19.93 D ATOM 8096 CD1 ILE D 577 127.641 5.922 43.008 1.00 20.62 D ATOM 8097 C ILE D 577 129.232 10.403 44.528 1.00 21.53 D ATOM 8098 O ILE D 577 128.603 10.777 45.530 1.00 23.56 D ATOM 8099 N TYR D 578 129.615 11.223 43.551 1.00 20.82 D ATOM 8100 CA TYR D 578 129.264 12.644 43.593 1.00 21.04 D ATOM 8101 CB TYR D 578 130.384 13.509 42.982 1.00 21.65 D ATOM 8102 CG TYR D 578 130.022 14.975 42.792 1.00 22.52 D ATOM 8103 CD1 TYR D 578 129.168 15.625 43.690 1.00 22.16 D ATOM 8104 CE1 TYR D 578 128.795 16.960 43.506 1.00 21.60 D ATOM 8105 CD2 TYR D 578 130.510 15.702 41.701 1.00 21.12 D ATOM 8106 CE2 TYR D 578 130.147 17.038 41.506 1.00 21.36 D ATOM 8107 CZ TYR D 578 129.286 17.663 42.410 1.00 21.53 D ATOM 8108 OH TYR D 578 128.900 18.977 42.212 1.00 21.71 D ATOM 8109 C TYR D 578 127.955 12.883 42.851 1.00 20.91 D ATOM 8110 O TYR D 578 127.939 12.885 41.633 1.00 21.83 D ATOM 8111 N ASP D 579 126.866 13.094 43.596 1.00 22.68 D ATOM 8112 CA ASP D 579 125.534 13.342 43.017 1.00 24.76 D ATOM 8113 CB ASP D 579 124.440 13.037 44.054 1.00 25.04 D ATOM 8114 CG ASP D 579 123.029 12.930 43.443 1.00 27.17 D ATOM 8115 OD1 ASP D 579 122.790 13.506 42.363 1.00 26.43 D ATOM 8116 OD2 ASP D 579 122.144 12.271 44.061 1.00 27.38 D ATOM 8117 C ASP D 579 125.435 14.808 42.583 1.00 26.38 D ATOM 8118 O ASP D 579 124.715 15.590 43.200 1.00 25.82 D ATOM 8119 N HIS D 580 126.148 15.172 41.513 1.00 28.39 D ATOM 8120 CA HIS D 580 126.145 16.555 41.028 1.00 31.78 D ATOM 8121 CB HIS D 580 127.029 16.692 39.794 1.00 33.03 D ATOM 8122 CG HIS D 580 126.607 15.830 38.654 1.00 37.41 D ATOM 8123 CD2 HIS D 580 125.611 15.973 37.750 1.00 38.10 D ATOM 8124 ND1 HIS D 580 127.244 14.648 38.342 1.00 39.09 D ATOM 8125 CE1 HIS D 580 126.660 14.102 37.292 1.00 38.85 D ATOM 8126 NE2 HIS D 580 125.666 14.885 36.913 1.00 39.22 D ATOM 8127 C HIS D 580 124.745 17.113 40.723 1.00 33.01 D ATOM 8128 O HIS D 580 124.484 18.313 40.890 1.00 34.71 D ATOM 8129 N GLU D 581 123.836 16.251 40.292 1.00 33.24 D ATOM 8130 CA GLU D 581 122.486 16.693 39.995 1.00 32.71 D ATOM 8131 CB GLU D 581 121.700 15.544 39.375 1.00 35.03 D ATOM 8132 CG GLU D 581 120.463 15.978 38.652 1.00 39.07 D ATOM 8133 CD GLU D 581 119.702 14.818 38.092 1.00 41.55 D ATOM 8134 OE1 GLU D 581 120.332 14.026 37.350 1.00 43.80 D ATOM 8135 OE2 GLU D 581 118.485 14.712 38.394 1.00 41.52 D ATOM 8136 C GLU D 581 121.788 17.202 41.266 1.00 31.80 D ATOM 8137 O GLU D 581 121.244 18.306 41.260 1.00 31.97 D ATOM 8138 N ARG D 582 121.808 16.414 42.348 1.00 29.57 D ATOM 8139 CA ARG D 582 121.177 16.825 43.616 1.00 29.36 D ATOM 8140 CB ARG D 582 120.622 15.607 44.390 1.00 26.09 D ATOM 8141 CG ARG D 582 119.558 14.822 43.650 1.00 22.04 D ATOM 8142 CD ARG D 582 118.850 13.766 44.496 1.00 20.11 D ATOM 8143 NE ARG D 582 118.024 12.908 43.636 1.00 19.38 D ATOM 8144 CZ ARG D 582 118.506 12.137 42.658 1.00 20.74 D ATOM 8145 NH1 ARG D 582 119.808 12.105 42.415 1.00 22.11 D ATOM 8146 NH2 ARG D 582 117.695 11.398 41.908 1.00 19.51 D ATOM 8147 C ARG D 582 122.160 17.598 44.531 1.00 31.40 D ATOM 8148 O ARG D 582 121.796 18.063 45.622 1.00 29.69 D ATOM 8149 N LYS D 583 123.401 17.747 44.074 1.00 33.89 D ATOM 8150 CA LYS D 583 124.433 18.436 44.849 1.00 35.05 D ATOM 8151 CB LYS D 583 124.069 19.912 45.068 1.00 38.08 D ATOM 8152 CG LYS D 583 124.348 20.830 43.882 1.00 40.35 D ATOM 8153 CD LYS D 583 125.842 20.963 43.611 1.00 42.80 D ATOM 8154 CE LYS D 583 126.103 21.734 42.310 1.00 42.80 D ATOM 8155 NZ LYS D 583 125.618 23.153 42.366 1.00 43.25 D ATOM 8156 C LYS D 583 124.627 17.755 46.202 1.00 34.05 D ATOM 8157 O LYS D 583 124.524 18.401 47.241 1.00 35.02 D ATOM 8158 N ARG D 584 124.898 16.449 46.172 1.00 33.23 D ATOM 8159 CA ARG D 584 125.128 15.634 47.370 1.00 31.46 D ATOM 8160 CB ARG D 584 123.854 14.861 47.768 1.00 29.44 D ATOM 8161 CG ARG D 584 122.595 15.702 47.938 1.00 30.45 D ATOM 8162 CD ARG D 584 121.369 14.815 48.175 1.00 30.86 D ATOM 8163 NE ARG D 584 120.098 15.542 48.113 1.00 31.46 D ATOM 8164 CZ ARG D 584 118.904 14.965 48.229 1.00 32.25 D ATOM 8165 NH1 ARG D 584 118.820 13.653 48.414 1.00 29.52 D ATOM 8166 NH2 ARG D 584 117.793 15.697 48.156 1.00 30.64 D ATOM 8167 C ARG D 584 126.247 14.622 47.065 1.00 31.14 D ATOM 8168 O ARG D 584 126.668 14.466 45.916 1.00 30.87 D ATOM 8169 N CYS D 585 126.732 13.961 48.111 1.00 30.50 D ATOM 8170 CA CYS D 585 127.762 12.937 48.009 1.00 29.49 D ATOM 8171 CB CYS D 585 129.086 13.427 48.598 1.00 32.51 D ATOM 8172 SG CYS D 585 130.268 12.081 49.098 1.00 36.50 D ATOM 8173 C CYS D 585 127.298 11.719 48.809 1.00 28.24 D ATOM 8174 O CYS D 585 126.814 11.850 49.943 1.00 28.12 D ATOM 8175 N ILE D 586 127.434 10.546 48.193 1.00 25.25 D ATOM 8176 CA ILE D 586 127.094 9.266 48.806 1.00 22.27 D ATOM 8177 CB ILE D 586 126.394 8.304 47.804 1.00 21.75 D ATOM 8178 CG2 ILE D 586 126.164 6.967 48.464 1.00 18.50 D ATOM 8179 CG1 ILE D 586 125.070 8.900 47.279 1.00 21.75 D ATOM 8180 CD1 ILE D 586 125.217 9.902 46.122 1.00 19.83 D ATOM 8181 C ILE D 586 128.460 8.670 49.123 1.00 22.41 D ATOM 8182 O ILE D 586 129.400 8.875 48.359 1.00 24.24 D ATOM 8183 N SER D 587 128.586 7.955 50.236 1.00 21.77 D ATOM 8184 CA SER D 587 129.856 7.319 50.595 1.00 19.65 D ATOM 8185 CB SER D 587 130.644 8.217 51.548 1.00 18.81 D ATOM 8186 OC SER D 587 129.942 8.436 52.758 1.00 17.09 D ATOM 8187 C SER D 587 129.579 5.968 51.255 1.00 19.73 D ATOM 8188 O SER D 587 128.676 5.867 52.082 1.00 20.77 D ATOM 8189 N ALA D 588 130.334 4.936 50.874 1.00 19.14 D ATOM 8190 CA ALA D 588 130.169 3.595 51.436 1.00 18.83 D ATOM 8191 CB ALA D 588 129.817 2.586 50.342 1.00 17.57 D ATOM 8192 C ALA D 588 131.483 3.220 52.105 1.00 18.48 D ATOM 8193 O ALA D 588 132.549 3.280 51.482 1.00 18.12 D ATOM 8194 N SER D 589 131.387 2.829 53.375 1.00 19.29 D ATOM 8195 CA SER D 589 132.546 2.500 54.224 1.00 20.33 D ATOM 8196 CB SER D 589 132.552 3.487 55.416 1.00 21.31 D ATOM 8197 OG SER D 589 133.427 3.106 56.474 1.00 19.54 D ATOM 8198 C SER D 589 132.633 1.058 54.749 1.00 20.03 D ATOM 8199 O SER D 589 131.638 0.322 54.743 1.00 20.59 D ATOM 8200 N MSE D 590 133.837 0.677 55.189 1.00 22.56 D ATOM 8201 CA MSE D 590 134.089 −0.644 55.760 1.00 25.48 D ATOM 8202 CB MSE D 590 135.578 −0.827 56.067 1.00 28.07 D ATOM 8203 CG MSE D 590 135.932 −2.225 56.531 1.00 30.40 D ATOM 8204 SE MSE D 590 137.843 −2.501 56.672 1.00 39.74 D ATOM 8205 CE MSE D 590 138.123 −3.610 55.120 1.00 33.01 D ATOM 8206 C MSE D 590 133.271 −0.777 57.053 1.00 26.26 D ATOM 8207 O MSE D 590 133.045 −1.883 57.540 1.00 27.96 D ATOM 8208 N ASP D 591 132.806 0.352 57.587 1.00 24.74 D ATOM 8209 CA ASP D 591 131.999 0.333 58.790 1.00 24.47 D ATOM 8210 CB ASP D 591 131.931 1.722 59.447 1.00 25.09 D ATOM 8211 CG ASP D 591 131.115 2.730 58.635 1.00 26.02 D ATOM 8212 OD1 ASP D 591 130.116 2.338 57.987 1.00 23.16 D ATOM 8213 OD2 ASP D 591 131.461 3.930 58.668 1.00 28.61 D ATOM 8214 C ASP D 591 130.575 −0.167 58.535 1.00 25.63 D ATOM 8215 O ASP D 591 129.731 −0.111 59.435 1.00 27.48 D ATOM 8216 N THR D 592 130.280 −0.612 57.315 1.00 24.13 D ATOM 8217 CA THR D 592 128.953 −1.144 57.027 1.00 23.60 D ATOM 8218 CB THR D 592 128.479 −2.010 58.217 1.00 23.93 D ATOM 8219 OG1 THR D 592 129.276 −3.197 58.290 1.00 24.58 D ATOM 8220 CG2 THR D 592 127.032 −2.388 58.071 1.00 25.94 D ATOM 8221 C THR D 592 127.858 −0.117 56.694 1.00 23.10 D ATOM 8222 O THR D 592 126.814 −0.466 56.131 1.00 23.01 D ATOM 8223 N THR D 593 128.086 1.146 57.020 1.00 21.17 D ATOM 8224 CA THR D 593 127.084 2.164 56.743 1.00 20.07 D ATOM 8225 CB THR D 593 127.097 3.238 57.829 1.00 19.96 D ATOM 8226 OG1 THR D 593 128.317 3.981 57.736 1.00 20.19 D ATOM 8227 CG2 THR D 593 127.012 2.601 59.205 1.00 20.49 D ATOM 8228 C THR D 593 127.303 2.861 55.400 1.00 20.54 D ATOM 8229 O THR D 593 128.282 2.602 54.705 1.00 20.50 D ATOM 8230 N ILE D 594 126.360 3.728 55.039 1.00 19.85 D ATOM 8231 CA ILE D 594 126.422 4.520 53.823 1.00 18.48 D ATOM 8232 CB ILE D 594 125.423 4.012 52.749 1.00 17.96 D ATOM 8233 CG2 ILE D 594 125.476 4.931 51.512 1.00 16.27 D ATOM 8234 CG1 ILE D 594 125.763 2.564 52.352 1.00 17.94 D ATOM 8235 CD1 ILE D 594 124.874 1.976 51.244 1.00 13.75 D ATOM 8236 C ILE D 594 126.013 5.920 54.297 1.00 20.05 D ATOM 8237 O ILE D 594 125.125 6.060 55.147 1.00 19.44 D ATOM 8238 N ARG D 595 126.661 6.961 53.787 1.00 21.73 D ATOM 8239 CA ARG D 595 126.294 8.304 54.229 1.00 24.25 D ATOM 8240 CE ARG D 595 127.380 8.898 55.133 1.00 26.38 D ATOM 8241 CG ARG D 595 127.485 8.261 56.508 1.00 27.19 D ATOM 8242 CD ARG D 595 128.489 9.003 57.373 1.00 29.27 D ATOM 8243 NE ARG D 595 128.184 8.848 58.797 1.00 33.82 D ATOM 8244 CZ ARG D 595 128.465 9.753 59.732 1.00 34.00 D ATOM 8245 NH1 ARG D 595 129.068 10.889 59.398 1.00 34.40 D ATOM 8246 NH2 ARG D 595 128.125 9.528 60.998 1.00 33.02 D ATOM 8247 C ARG D 595 125.999 9.282 53.108 1.00 24.90 D ATOM 8248 O ARG D 595 126.702 9.329 52.102 1.00 25.43 D ATOM 8249 N ILE D 596 124.939 10.056 53.294 1.00 25.81 D ATOM 8250 CA ILE D 596 124.540 11.056 52.319 1.00 27.39 D ATOM 8251 CB ILE D 596 123.000 11.093 52.138 1.00 27.40 D ATOM 8252 CG2 ILE D 596 122.646 11.950 50.935 1.00 27.77 D ATOM 8253 CG1 ILE D 596 122.459 9.681 51.891 1.00 27.13 D ATOM 8254 CD1 ILE D 596 122.953 9.062 50.590 1.00 26.64 D ATOM 8255 C ILE D 596 125.013 12.392 52.870 1.00 28.16 D ATOM 8256 O ILE D 596 124.637 12.787 53.976 1.00 28.61 D ATOM 8257 N TRP D 597 125.862 13.078 52.118 1.00 28.67 D ATOM 8258 CA TRP D 597 126.368 14.368 52.568 1.00 28.04 D ATOM 8259 CE TRP D 597 127.893 14.391 52.515 1.00 29.61 D ATOM 8260 CG TRP D 597 128.562 13.228 53.155 1.00 28.57 D ATOM 8261 CD2 TRP D 597 129.116 13.186 54.470 1.00 27.43 D ATOM 8262 CE2 TRP D 597 129.707 11.918 54.634 1.00 27.37 D ATOM 8263 CE3 TRP D 597 129.172 14.103 55.529 1.00 27.46 D ATOM 8264 CD1 TRP D 597 128.822 12.016 52.589 1.00 29.00 D ATOM 8265 NE1 TRP D 597 129.516 11.221 53.469 1.00 27.32 D ATOM 8266 CZ2 TRP D 597 130.349 11.541 55.817 1.00 27.76 D ATOM 8267 CZ3 TRP D 597 129.810 13.729 56.703 1.00 27.02 D ATOM 8268 CR2 TRP D 597 130.389 12.457 56.838 1.00 27.58 D ATOM 8269 C TRP D 597 125.838 15.486 51.684 1.00 27.75 D ATOM 8270 O TRP D 597 125.729 15.326 50.472 1.00 27.73 D ATOM 8271 N ASP D 598 125.519 16.624 52.284 1.00 28.69 D ATOM 8272 CA ASP D 598 125.012 17.773 51.527 1.00 29.82 D ATOM 8273 CB ASP D 598 123.966 18.511 52.381 1.00 29.96 D ATOM 8274 CG ASP D 598 123.483 19.816 51.749 1.00 30.01 D ATOM 8275 OD1 ASP D 598 123.889 20.118 50.601 1.00 29.40 D ATOM 8276 OD2 ASP D 598 122.700 20.537 52.417 1.00 28.15 D ATOM 8277 C ASP D 598 126.197 18.694 51.177 1.00 28.75 D ATOM 8278 O ASP D 598 126.880 19.192 52.067 1.00 26.58 D ATOM 8279 N LEU D 599 126.442 18.912 49.884 1.00 29.62 D ATOM 8280 CA LEU D 599 127.567 19.753 49.466 1.00 32.72 D ATOM 8281 CB LEU D 599 128.148 19.244 48.141 1.00 30.82 D ATOM 8282 CG LEU D 599 128.646 17.780 48.141 1.00 31.03 D ATOM 8283 CD1 LEU D 599 129.360 17.472 46.822 1.00 29.75 D ATOM 8284 CD2 LEU D 599 129.579 17.529 49.309 1.00 28.77 D ATOM 8285 C LEU D 599 127.238 21.246 49.383 1.00 35.04 D ATOM 8286 O LEU D 599 127.899 22.009 48.686 1.00 34.05 D ATOM 8287 N GLU D 600 126.228 21.651 50.145 1.00 39.89 D ATOM 8288 CA GLU D 600 125.793 23.041 50.205 1.00 42.71 D ATOM 8289 CB GLU D 600 124.279 23.118 49.998 1.00 43.83 D ATOM 8290 CG GLU D 600 123.818 22.578 48.659 1.00 49.15 D ATOM 8291 CD GLU D 600 124.057 23.565 47.524 1.00 52.47 D ATOM 8292 OE1 GLU D 600 123.836 23.205 46.340 1.00 54.37 D ATOM 8293 OE2 GLU D 600 124.462 24.710 47.820 1.00 53.81 D ATOM 8294 C GLU D 600 126.154 23.614 51.581 1.00 43.08 D ATOM 8295 O GLU D 600 125.956 24.799 51.847 1.00 44.92 D ATOM 8296 N ASN D 605 126.681 22.769 52.461 1.00 42.60 D ATOM 8297 CA ASN D 605 127.049 23.217 53.798 1.00 41.25 D ATOM 8298 CB ASN D 605 125.787 23.392 54.640 1.00 41.21 D ATOM 8299 CG ASN D 605 125.003 22.105 54.794 1.00 42.82 D ATOM 8300 OD1 ASN D 605 124.753 21.383 53.830 1.00 41.44 D ATOM 8301 ND2 ASN D 605 124.599 21.819 56.024 1.00 44.97 D ATOM 8302 C ASN D 605 128.006 22.222 54.440 1.00 40.16 D ATOM 8303 O ASN D 605 128.507 22.442 55.544 1.00 39.89 D ATOM 8304 N GLY D 606 128.259 21.135 53.712 1.00 39.38 D ATOM 8305 CA GLY D 606 129.165 20.091 54.156 1.00 36.83 D ATOM 8306 C GLY D 606 128.629 19.279 55.311 1.00 35.89 D ATOM 8307 O GLY D 606 129.336 18.446 55.865 1.00 35.05 D ATOM 8308 N GLU D 607 127.378 19.523 55.675 1.00 35.04 D ATOM 8309 CA GLU D 607 126.771 18.814 56.779 1.00 35.34 D ATOM 8310 CB GLU D 607 125.624 19.635 57.350 1.00 38.59 D ATOM 8311 CG GLU D 607 126.032 20.652 58.401 1.00 44.13 D ATOM 8312 CD GLU D 607 124.828 21.150 59.183 1.00 49.69 D ATOM 8313 OE1 GLU D 607 124.093 20.289 59.749 1.00 51.01 D ATOM 8314 OE2 GLU D 607 124.608 22.394 59.227 1.00 52.33 D ATOM 8315 C GLU D 607 126.271 17.415 56.411 1.00 33.71 D ATOM 8316 O GLU D 607 125.991 17.144 55.247 1.00 33.25 D ATOM 8317 N LEU D 608 126.175 16.521 57.397 1.00 31.85 D ATOM 8318 CA LEU D 608 125.686 15.175 57.125 1.00 30.51 D ATOM 8319 CE LEU D 608 126.052 14.216 58.253 1.00 27.96 D ATOM 8320 CG LEU D 608 125.557 12.778 58.041 1.00 28.56 D ATOM 8321 CD1 LEU D 608 126.456 12.051 57.046 1.00 24.69 D ATOM 8322 CD2 LEU D 608 125.531 12.032 59.394 1.00 28.82 D ATOM 8323 C LEU D 608 124.169 15.253 56.971 1.00 30.57 D ATOM 8324 O LEU D 608 123.532 16.124 57.573 1.00 31.18 D ATOM 8325 N MEE D 625 123.605 14.363 56.150 1.00 29.87 D ATOM 8326 CA MSE D 625 122.153 14.303 55.888 1.00 30.31 D ATOM 8327 CB MSE D 625 121.846 14.367 54.381 1.00 31.08 D ATOM 8328 CG MSE D 625 122.016 15.737 53.754 1.00 33.02 D ATOM 8329 SE MSE D 625 121.598 15.802 51.862 1.00 38.72 D ATOM 8330 CE MSE D 625 119.705 15.354 51.962 1.00 32.55 D ATOM 8331 C MSE D 625 121.523 13.022 56.410 1.00 27.88 D ATOM 8332 O MSE D 625 120.538 13.032 57.145 1.00 28.06 D ATOM 8333 N TYR D 626 122.073 11.901 55.993 1.00 25.99 D ATOM 8334 CA TYR D 626 121.505 10.670 56.444 1.00 24.99 D ATOM 8335 CB TYR D 626 120.453 10.176 55.461 1.00 25.25 D ATOM 8336 CG TYR D 626 119.434 11.186 54.999 1.00 24.62 D ATOM 8337 CD1 TYR D 626 118.409 11.612 55.842 1.00 21.86 D ATOM 8338 CE1 TYR D 626 117.391 12.424 55.363 1.00 23.49 D ATOM 8339 CD2 TYR D 626 119.426 11.615 53.669 1.00 24.69 D ATOM 8340 CE2 TYR D 626 118.421 12.421 53.179 1.00 24.51 D ATOM 8341 CZ TYR D 626 117.396 12.820 54.023 1.00 24.72 D ATOM 8342 OH TYR D 626 116.346 13.555 53.502 1.00 25.76 D ATOM 8343 C TYR D 626 122.555 9.597 56.565 1.00 23.88 D ATOM 8344 O TYR D 626 123.605 9.652 55.923 1.00 23.89 D ATOM 8345 N THR D 627 122.255 8.616 57.406 1.00 23.42 D ATOM 8346 CA THR D 627 123.122 7.472 57.564 1.00 20.62 D ATOM 8347 CE THR D 627 123.589 7.271 58.987 1.00 19.43 D ATOM 8348 OG1 THR D 627 124.268 8.447 59.440 1.00 20.14 D ATOM 8349 CG2 THR D 627 124.535 6.066 59.050 1.00 17.31 D ATOM 8350 C THR D 627 122.235 6.308 57.191 1.00 19.41 D ATOM 8351 O THR D 627 121.244 6.050 57.859 1.00 18.63 D ATOM 8352 N LEU D 628 122.577 5.640 56.095 1.00 19.47 D ATOM 8353 CA LEU D 628 121.821 4.485 55.626 1.00 19.11 D ATOM 8354 CE LEU D 628 121.755 4.469 54.108 1.00 17.80 D ATOM 8355 CG LEU D 628 121.117 5.669 53.396 1.00 16.59 D ATOM 8356 CD1 LEU D 628 121.092 5.364 51.890 1.00 16.34 D ATOM 8357 CD2 LEU D 628 119.712 5.929 53.916 1.00 13.86 D ATOM 8358 C LEU D 628 122.523 3.227 56.111 1.00 19.57 D ATOM 8359 O LEU D 628 123.674 2.966 55.744 1.00 20.61 D ATOM 8360 N GLN D 629 121.817 2.456 56.936 1.00 19.21 D ATOM 8361 CA GLN D 629 122.331 1.216 57.512 1.00 19.59 D ATOM 8362 CE GLN D 629 122.142 1.262 59.031 1.00 18.99 D ATOM 8363 CG GLN D 629 122.640 0.047 59.795 1.00 19.95 D ATOM 8364 CD GLN D 629 124.155 −0.088 59.756 1.00 21.73 D ATOM 8365 OE1 GLN D 629 124.709 −0.697 58.841 1.00 21.66 D ATOM 8366 NE2 GLN D 629 124.834 0.492 60.751 1.00 21.48 D ATOM 8367 C GLN D 629 121.565 0.034 56.922 1.00 19.26 D ATOM 8368 O GLN D 629 120.435 −0.224 57.313 1.00 22.24 D ATOM 8369 N GLY D 630 122.178 −0.689 55.993 1.00 18.64 D ATOM 8370 CA GLY D 630 121.480 −1.802 55.386 1.00 19.70 D ATOM 8371 C GLY D 630 122.361 −2.917 54.860 1.00 21.44 D ATOM 8372 O GLY D 630 122.068 −3.533 53.844 1.00 22.81 D ATOM 8373 N HIS D 631 123.459 −3.179 55.544 1.00 22.39 D ATOM 8374 CA HIS D 631 124.368 −4.236 55.143 1.00 23.12 D ATOM 8375 CB HIS D 631 125.425 −3.720 54.169 1.00 26.25 D ATOM 8376 CG HIS D 631 124.856 −3.144 52.915 1.00 28.65 D ATOM 8377 CD2 HIS D 631 124.544 −1.870 52.586 1.00 28.78 D ATOM 8378 ND1 HIS D 631 124.504 −3.920 51.833 1.00 29.43 D ATOM 8379 CE1 HIS D 631 124.002 −3.146 50.887 1.00 28.34 D ATOM 8380 NE2 HIS D 631 124.015 −1.898 51.319 1.00 28.49 D ATOM 8381 C HIS D 631 125.030 −4.618 56.440 1.00 22.81 D ATOM 8382 O HIS D 631 125.008 −3.860 57.402 1.00 25.35 D ATOM 8383 N THR D 632 125.661 −5.774 56.455 1.00 21.41 D ATOM 8384 CA THR D 632 126.288 −6.261 57.663 1.00 20.28 D ATOM 8385 CB THR D 632 125.646 −7.591 58.047 1.00 18.49 D ATOM 8386 OG1 THR D 632 125.767 −8.524 56.957 1.00 18.30 D ATOM 8387 CG2 THR D 632 124.173 −7.371 58.349 1.00 13.99 D ATOM 8388 C THR D 632 127.771 −6.466 57.509 1.00 20.33 D ATOM 8389 O THR D 632 128.427 −6.983 58.405 1.00 22.76 D ATOM 8390 N ALA D 633 128.291 −6.053 56.367 1.00 19.78 D ATOM 8391 CA ALA D 633 129.695 −6.224 56.061 1.00 18.83 D ATOM 8392 CB ALA D 633 129.877 −7.469 55.239 1.00 17.26 D ATOM 8393 C ALA D 633 130.169 −5.029 55.282 1.00 19.55 D ATOM 8394 O ALA D 633 129.385 −4.126 54.991 1.00 19.68 D ATOM 8395 N LEU D 634 131.455 −5.024 54.951 1.00 20.72 D ATOM 8396 CA LEU D 634 132.051 −3.944 54.175 1.00 20.81 D ATOM 8397 CB LEU D 634 133.478 −4.347 53.790 1.00 21.47 D ATOM 8398 CG LEU D 634 134.286 −3.752 52.639 1.00 22.59 D ATOM 8399 CD1 LEU D 634 133.982 −4.534 51.395 1.00 25.22 D ATOM 8400 CD2 LEU D 634 133.968 −2.263 52.448 1.00 26.73 D ATOM 8401 C LEU D 634 131.211 −3.634 52.940 1.00 21.70 D ATOM 8402 O LEU D 634 130.889 −4.523 52.138 1.00 22.37 D ATOM 8403 N VAL D 635 130.822 −2.371 52.807 1.00 21.89 D ATOM 8404 CA VAL D 635 130.038 −1.957 51.646 1.00 23.38 D ATOM 8405 CB VAL D 635 128.929 −0.951 52.019 1.00 23.26 D ATOM 8406 CG1 VAL D 635 128.136 −0.574 50.771 1.00 25.04 D ATOM 8407 CG2 VAL D 635 128.008 −1.545 53.048 1.00 21.55 D ATOM 8408 C VAL D 635 131.019 −1.303 50.670 1.00 24.61 D ATOM 8409 O VAL D 635 131.455 −0.164 50.878 1.00 22.67 D ATOM 8410 N GLY D 636 131.352 −2.036 49.607 1.00 25.64 D ATOM 8411 CA GLY D 636 132.320 −1.552 48.641 1.00 26.53 D ATOM 8412 C GLY D 636 131.874 −1.151 47.254 1.00 26.66 D ATOM 8413 O GLY D 636 132.687 −0.595 46.509 1.00 27.11 D ATOM 8414 N LEU D 637 130.612 −1.418 46.906 1.00 26.43 D ATOM 8415 CA LEU D 637 130.077 −1.089 45.582 1.00 24.26 D ATOM 8416 CB LEU D 637 129.705 −2.367 44.825 1.00 22.49 D ATOM 8417 CG LEU D 637 130.896 −3.277 44.542 1.00 21.34 D ATOM 8418 CD1 LEU D 637 132.028 −2.399 44.003 1.00 18.59 D ATOM 8419 CD2 LEU D 637 131.352 −3.982 45.809 1.00 23.19 D ATOM 8420 C LEU D 637 128.868 −0.163 45.606 1.00 25.18 D ATOM 8421 O LEU D 637 127.843 −0.503 46.182 1.00 26.31 D ATOM 8422 N LEU D 638 129.009 1.004 44.970 1.00 26.27 D ATOM 8423 CA LEU D 638 127.959 2.021 44.854 1.00 25.24 D ATOM 8424 CB LEU D 638 128.335 3.308 45.579 1.00 25.17 D ATOM 8425 CG LEU D 638 128.217 3.292 47.092 1.00 26.38 D ATOM 8426 CD1 LEU D 638 128.445 4.708 47.617 1.00 25.29 D ATOM 8427 CD2 LEU D 638 126.827 2.778 47.484 1.00 23.90 D ATOM 8428 C LEU D 638 127.772 2.372 43.396 1.00 25.47 D ATOM 8429 O LEU D 638 128.746 2.427 42.638 1.00 24.74 D ATOM 8430 N ARG D 639 126.515 2.639 43.029 1.00 25.82 D ATOM 8431 CA ARG D 639 126.101 2.999 41.661 1.00 24.67 D ATOM 8432 CB ARG D 639 125.735 1.733 40.875 1.00 24.23 D ATOM 8433 CG ARG D 639 126.472 1.524 39.569 1.00 24.13 D ATOM 8434 CD ARG D 639 127.923 1.341 39.843 1.00 24.24 D ATOM 8435 NE ARG D 639 128.539 0.275 39.061 1.00 25.29 D ATOM 8436 CZ ARG D 639 129.345 0.488 38.027 1.00 26.83 D ATOM 8437 NH1 ARG D 639 129.609 1.735 37.658 1.00 22.95 D ATOM 8438 NH2 ARG D 639 129.909 −0.538 37.387 1.00 27.61 D ATOM 8439 C ARG D 639 124.857 3.877 41.777 1.00 24.76 D ATOM 8440 O ARG D 639 123.942 3.540 42.519 1.00 24.70 D ATOM 8441 N LEU D 640 124.821 4.991 41.046 1.00 25.49 D ATOM 8442 CA LEU D 640 123.668 5.908 41.066 1.00 23.58 D ATOM 8443 CB LEU D 640 124.142 7.354 41.250 1.00 20.68 D ATOM 8444 CG LEU D 640 123.301 8.220 42.178 1.00 21.27 D ATOM 8445 CD1 LEU D 640 123.483 9.698 41.849 1.00 19.99 D ATOM 8446 CD2 LEU D 640 121.854 7.834 42.058 1.00 21.23 D ATOM 8447 C LEU D 640 122.888 5.800 39.753 1.00 23.09 D ATOM 8448 O LEU D 640 123.464 5.886 38.677 1.00 25.33 D ATOM 8449 N SER D 641 121.582 5.598 39.846 1.00 22.47 D ATOM 8450 CA SER D 641 120.741 5.498 38.668 1.00 21.80 D ATOM 8451 CB SER D 641 119.920 4.212 38.713 1.00 23.05 D ATOM 8452 OC SER D 641 118.628 4.399 38.170 1.00 26.20 D ATOM 8453 C SER D 641 119.837 6.712 38.706 1.00 22.79 D ATOM 8454 O SER D 641 119.697 7.344 39.743 1.00 21.44 D ATOM 8455 N ASP D 642 119.206 7.052 37.596 1.00 25.87 D ATOM 8456 CA ASP D 642 118.361 8.230 37.631 1.00 29.02 D ATOM 8457 CB ASP D 642 117.753 8.507 36.258 1.00 32.11 D ATOM 8458 CG ASP D 642 117.066 9.854 36.206 1.00 35.97 D ATOM 8459 OD1 ASP D 642 117.782 10.877 36.333 1.00 38.30 D ATOM 8460 OD2 ASP D 642 115.817 9.904 36.059 1.00 37.81 D ATOM 8461 C ASP D 642 117.247 8.077 38.655 1.00 28.71 D ATOM 8462 O ASP D 642 116.649 9.055 39.098 1.00 28.83 D ATOM 8463 N LYS D 643 116.975 6.847 39.047 1.00 29.24 D ATOM 8464 CA LYS D 643 115.903 6.626 39.989 1.00 29.96 D ATOM 8465 CB LYS D 643 114.760 5.934 39.241 1.00 31.36 D ATOM 8466 CG LYS D 643 113.626 5.382 40.076 1.00 36.57 D ATOM 8467 CD LYS D 643 112.491 4.792 39.183 1.00 38.95 D ATOM 8468 CE LYS D 643 111.899 5.844 38.222 1.00 40.27 D ATOM 8469 NZ LYS D 643 110.719 5.330 37.453 1.00 40.99 D ATOM 8470 C LYS D 643 116.325 5.831 41.222 1.00 29.02 D ATOM 8471 O LYS D 643 115.628 5.832 42.234 1.00 29.30 D ATOM 8472 N PHE D 644 117.483 5.187 41.160 1.00 27.45 D ATOM 8473 CA PHE D 644 117.924 4.370 42.276 1.00 25.90 D ATOM 8474 CB PHE D 644 117.822 2.889 41.918 1.00 23.62 D ATOM 8475 CG PHE D 644 116.428 2.416 41.670 1.00 22.94 D ATOM 8476 CD1 PHE D 644 116.097 1.784 40.480 1.00 23.53 D ATOM 8477 CD2 PHE D 644 115.448 2.567 42.632 1.00 21.03 D ATOM 8478 CE1 PHE D 644 114.807 1.309 40.266 1.00 21.81 D ATOM 8479 CE2 PHE D 644 114.164 2.094 42.416 1.00 18.29 D ATOM 8480 CZ PHE D 644 113.847 1.467 41.237 1.00 17.27 D ATOM 8481 C PHE D 644 119.337 4.618 42.735 1.00 26.43 D ATOM 8482 O PHE D 644 120.164 5.136 41.989 1.00 25.68 D ATOM 8483 N LEU D 645 119.589 4.238 43.988 1.00 27.14 D ATOM 8484 CA LEU D 645 120.911 4.318 44.608 1.00 26.31 D ATOM 8485 CB LEU D 645 120.914 5.234 45.828 1.00 27.08 D ATOM 8486 CG LEU D 645 122.217 5.194 46.640 1.00 27.94 D ATOM 8487 CD1 LEU D 645 123.290 5.975 45.918 1.00 29.78 D ATOM 8488 CD2 LEU D 645 121.994 5.766 48.028 1.00 27.68 D ATOM 8489 C LEU D 645 121.152 2.890 45.059 1.00 24.69 D ATOM 8490 O LEU D 645 120.758 2.514 46.146 1.00 26.35 D ATOM 8491 N VAL D 646 121.786 2.100 44.206 1.00 23.16 D ATOM 8492 CA VAL D 646 122.056 0.706 44.499 1.00 21.12 D ATOM 8493 CB VAL D 646 122.116 −0.101 43.212 1.00 20.50 D ATOM 8494 CG1 VAL D 646 122.047 −1.583 43.514 1.00 21.04 D ATOM 8495 CG2 VAL D 646 120.997 0.334 42.283 1.00 20.61 D ATOM 8496 C VAL D 646 123.384 0.523 45.211 1.00 20.80 D ATOM 8497 O VAL D 646 124.375 1.159 44.857 1.00 21.52 D ATOM 8498 N SER D 647 123.408 −0.356 46.208 1.00 20.76 D ATOM 8499 CA SER D 647 124.637 −0.643 46.936 1.00 19.72 D ATOM 8500 CB SER D 647 124.706 0.166 48.231 1.00 19.38 D ATOM 8501 OG SER D 647 123.594 −0.100 49.071 1.00 20.83 D ATOM 8502 C SER D 647 124.723 −2.140 47.249 1.00 19.78 D ATOM 8503 O SER D 647 123.694 −2.816 47.373 1.00 18.23 D ATOM 8504 N ALA D 648 125.950 −2.654 47.344 1.00 18.94 D ATOM 8505 CA ALA D 648 126.175 −4.060 47.646 1.00 19.09 D ATOM 8506 CB ALA D 648 126.463 −4.850 46.377 1.00 15.72 D ATOM 8507 C ALA D 648 127.337 −4.180 48.618 1.00 20.74 D ATOM 8508 O ALA D 648 128.279 −3.399 48.547 1.00 22.53 D ATOM 8509 N ALA D 649 127.253 −5.148 49.533 1.00 21.16 D ATOM 8510 CA ALA D 649 128.301 −5.372 50.514 1.00 20.36 D ATOM 8511 CB ALA D 649 127.774 −5.097 51.911 1.00 23.59 D ATOM 8512 C ALA D 649 128.912 −6.772 50.457 1.00 20.64 D ATOM 8513 O ALA D 649 128.453 −7.663 49.723 1.00 19.52 D ATOM 8514 N ALA D 650 129.951 −6.944 51.271 1.00 18.79 D ATOM 8515 CA ALA D 650 130.703 −8.192 51.372 1.00 17.83 D ATOM 8516 CB ALA D 650 131.839 −8.012 52.334 1.00 17.25 D ATOM 8517 C ALA D 650 129.889 −9.409 51.786 1.00 17.38 D ATOM 8518 O ALA D 650 130.337 −10.545 51.626 1.00 16.75 D ATOM 8519 N ASP D 651 128.699 −9.190 52.329 1.00 18.32 D ATOM 8520 CA ASP D 651 127.880 −10.323 52.748 1.00 19.29 D ATOM 8521 CB ASP D 651 126.982 −9.930 53.920 1.00 21.96 D ATOM 8522 CG ASP D 651 126.027 −8.804 53.568 1.00 26.40 D ATOM 8523 OD1 ASP D 651 125.508 −8.816 52.425 1.00 28.33 D ATOM 8524 OD2 ASP D 651 125.781 −7.924 54.436 1.00 25.72 D ATOM 8525 C ASP D 651 127.026 −10.856 51.609 1.00 19.07 D ATOM 8526 O ASP D 651 126.244 −11.789 51.787 1.00 20.37 D ATOM 8527 N GLY D 652 127.164 −10.256 50.437 1.00 19.11 D ATOM 8528 CA GLY D 652 126.370 −10.711 49.315 1.00 18.71 D ATOM 8529 C GLY D 652 125.024 −10.018 49.213 1.00 18.78 D ATOM 8530 O GLY D 652 124.142 −10.475 48.479 1.00 17.99 D ATOM 8531 N SER D 653 124.841 −8.926 49.950 1.00 20.24 D ATOM 8532 CA SER D 653 123.575 −8.198 49.864 1.00 21.58 D ATOM 8533 CB SER D 653 123.133 −7.678 51.236 1.00 21.54 D ATOM 8534 OG SER D 653 124.037 −6.731 51.772 1.00 22.98 D ATOM 8535 C SER D 653 123.665 −7.033 48.881 1.00 22.14 D ATOM 8536 O SER D 653 124.742 −6.510 48.598 1.00 21.79 D ATOM 8537 N ILE D 654 122.515 −6.652 48.350 1.00 23.25 D ATOM 8538 CA ILE D 654 122.418 −5.554 47.409 1.00 25.80 D ATOM 8539 CB ILE D 654 122.165 −6.055 45.982 1.00 26.21 D ATOM 8540 CG2 ILE D 654 122.297 −4.918 45.003 1.00 26.27 D ATOM 8541 CG1 ILE D 654 123.154 −7.158 45.616 1.00 28.16 D ATOM 8542 CD1 ILE D 654 122.870 −7.785 44.254 1.00 28.37 D ATOM 8543 C ILE D 654 121.197 −4.754 47.836 1.00 26.75 D ATOM 8544 O ILE D 654 120.122 −5.323 48.064 1.00 27.01 D ATOM 8545 N ARG D 655 121.346 −3.443 47.951 1.00 27.07 D ATOM 8546 CA ARG D 655 120.216 −2.626 48.356 1.00 27.67 D ATOM 8547 CB ARG D 655 120.467 −2.029 49.737 1.00 28.04 D ATOM 8548 CG ARG D 655 120.592 −3.062 50.832 1.00 29.00 D ATOM 8549 CD ARG D 655 119.901 −2.605 52.103 1.00 31.71 D ATOM 8550 NE ARG D 655 118.574 −3.199 52.240 1.00 33.84 D ATOM 8551 CZ ARG D 655 118.328 −4.314 52.914 1.00 33.80 D ATOM 8552 NH1 ARG D 655 119.314 −4.960 53.527 1.00 33.02 D ATOM 8553 NH2 ARG D 655 117.094 −4.787 52.953 1.00 36.00 D ATOM 8554 C ARG D 655 119.903 −1.524 47.358 1.00 27.31 D ATOM 8555 O ARG D 655 120.797 −0.985 46.706 1.00 26.04 D ATOM 8556 N GLY D 656 118.620 −1.203 47.237 1.00 27.56 D ATOM 8557 CA GLY D 656 118.206 −0.164 46.315 1.00 28.15 D ATOM 8558 C GLY D 656 117.482 0.916 47.087 1.00 27.66 D ATOM 8559 O GLY D 656 116.514 0.621 47.775 1.00 28.41 D ATOM 8560 N TRP D 657 117.944 2.158 46.996 1.00 27.78 D ATOM 8561 CA TRP D 657 117.299 3.256 47.715 1.00 28.29 D ATOM 8562 CB TRP D 657 118.296 3.913 48.699 1.00 26.47 D ATOM 8563 CG TRP D 657 119.251 2.947 49.419 1.00 24.99 D ATOM 8564 CD2 TRP D 657 119.136 2.448 50.768 1.00 23.38 D ATOM 8565 CE2 TRP D 657 120.215 1.554 50.972 1.00 22.65 D ATOM 8566 CE3 TRP D 657 118.226 2.664 51.818 1.00 22.66 D ATOM 8567 CD1 TRP D 657 120.369 2.352 48.891 1.00 22.06 D ATOM 8568 NE1 TRP D 657 120.947 1.520 49.815 1.00 21.92 D ATOM 8569 CZ2 TRP D 657 120.407 0.875 52.180 1.00 20.78 D ATOM 8570 CZ3 TRP D 657 118.423 1.979 53.026 1.00 22.09 D ATOM 8571 CR2 TRP D 657 119.505 1.098 53.187 1.00 22.26 D ATOM 8572 C TRP D 657 116.777 4.313 46.705 1.00 29.51 D ATOM 8573 O TRP D 657 117.304 4.422 45.592 1.00 29.88 D ATOM 8574 N ASP D 658 115.744 5.076 47.075 1.00 29.21 D ATOM 8575 CA ASP D 658 115.223 6.104 46.174 1.00 29.96 D ATOM 8576 CB ASP D 658 113.977 6.790 46.757 1.00 28.48 D ATOM 8577 CG ASP D 658 113.460 7.923 45.868 1.00 28.43 D ATOM 8578 OD1 ASP D 658 112.888 7.650 44.793 1.00 28.91 D ATOM 8579 OD2 ASP D 658 113.628 9.101 46.236 1.00 27.59 D ATOM 8580 C ASP D 658 116.354 7.113 46.026 1.00 31.50 D ATOM 8581 O ASP D 658 116.978 7.503 47.017 1.00 32.96 D ATOM 8582 N ALA D 659 116.621 7.526 44.791 1.00 31.88 D ATOM 8583 CA ALA D 659 117.694 8.468 44.499 1.00 32.44 D ATOM 8584 CB ALA D 659 117.811 8.649 43.010 1.00 32.07 D ATOM 8585 C ALA D 659 117.541 9.829 45.162 1.00 33.56 D ATOM 8586 O ALA D 659 118.463 10.634 45.141 1.00 34.05 D ATOM 8587 N ASN D 660 116.387 10.091 45.761 1.00 36.44 D ATOM 8588 CA ASN D 660 116.155 11.379 46.400 1.00 37.59 D ATOM 8589 CB ASN D 660 115.061 12.130 45.645 1.00 39.91 D ATOM 8590 CG ASN D 660 114.872 13.542 46.149 1.00 43.39 D ATOM 8591 OD1 ASN D 660 114.382 13.764 47.264 1.00 44.43 D ATOM 8592 ND2 ASN D 660 115.274 14.515 45.334 1.00 45.95 D ATOM 8593 C ASN D 660 115.791 11.248 47.876 1.00 36.76 D ATOM 8594 O ASN D 660 116.233 12.050 48.689 1.00 38.43 D ATOM 8595 N ASP D 661 114.991 10.239 48.214 1.00 35.26 D ATOM 8596 CA ASP D 661 114.566 9.984 49.592 1.00 33.16 D ATOM 8597 CB ASP D 661 113.165 9.393 49.620 1.00 34.45 D ATOM 8598 CG ASP D 661 112.144 10.331 49.104 1.00 38.11 D ATOM 8599 OD1 ASP D 661 112.280 11.540 49.419 1.00 40.95 D ATOM 8600 OD2 ASP D 661 111.200 9.876 48.409 1.00 39.95 D ATOM 8601 C ASP D 661 115.458 8.980 50.292 1.00 31.13 D ATOM 8602 O ASP D 661 115.569 9.004 51.505 1.00 31.79 D ATOM 8603 N TYR D 662 116.023 8.062 49.517 1.00 26.92 D ATOM 8604 CA TYR D 662 116.885 7.016 50.027 1.00 25.03 D ATOM 8605 CB TYR D 662 118.028 7.615 50.876 1.00 23.52 D ATOM 8606 CG TYR D 662 118.839 8.622 50.075 1.00 24.99 D ATOM 8607 CD1 TYR D 662 119.614 8.201 48.999 1.00 23.45 D ATOM 8608 CE1 TYR D 662 120.257 9.099 48.181 1.00 23.80 D ATOM 8609 CD2 TYR D 662 118.739 9.996 50.317 1.00 23.15 D ATOM 8610 CE2 TYR D 662 119.384 10.914 49.497 1.00 24.08 D ATOM 8611 CZ TYR D 662 120.143 10.459 48.424 1.00 25.80 D ATOM 8612 OH TYR D 662 120.770 11.367 47.581 1.00 25.60 D ATOM 8613 C TYR D 662 116.090 5.979 50.808 1.00 24.80 D ATOM 8614 O TYR D 662 116.663 5.210 51.590 1.00 25.89 D ATOM 8615 N SER D 663 114.777 5.946 50.575 1.00 21.66 D ATOM 8616 CA SER D 663 113.886 4.981 51.228 1.00 21.07 D ATOM 8617 CB SER D 663 112.432 5.460 51.165 1.00 20.52 D ATOM 8618 OG SER D 663 111.987 5.642 49.838 1.00 19.13 D ATOM 8619 C SER D 663 113.996 3.610 50.564 1.00 20.63 D ATOM 8620 O SER D 663 114.182 3.530 49.357 1.00 20.77 D ATOM 8621 N ARG D 664 113.901 2.537 51.353 1.00 21.12 D ATOM 8622 CA ARG D 664 114.022 1.180 50.819 1.00 20.22 D ATOM 8623 CB ARG D 664 113.564 0.125 51.849 1.00 22.66 D ATOM 8624 CG ARG D 664 114.575 −0.302 52.980 1.00 25.13 D ATOM 8625 CD ARG D 664 114.860 0.821 53.987 1.00 27.71 D ATOM 8626 NE ARG D 664 115.573 0.440 55.219 1.00 29.68 D ATOM 8627 CZ ARG D 664 116.626 −0.373 55.291 1.00 31.69 D ATOM 8628 NH1 ARG D 664 117.114 −0.935 54.200 1.00 34.72 D ATOM 8629 NH2 ARG D 664 117.226 −0.597 56.456 1.00 30.46 D ATOM 8630 C ARG D 664 113.196 1.037 49.552 1.00 18.91 D ATOM 8631 O ARG D 664 112.013 1.393 49.525 1.00 19.59 D ATOM 8632 N LYS D 665 113.833 0.544 48.496 1.00 17.43 D ATOM 8633 CA LYS D 665 113.144 0.320 47.238 1.00 16.40 D ATOM 8634 CB LYS D 665 113.729 1.204 46.148 1.00 14.06 D ATOM 8635 CG LYS D 665 113.132 2.582 46.190 1.00 13.78 D ATOM 8636 CD LYS D 665 111.661 2.434 45.960 1.00 14.84 D ATOM 8637 CE LYS D 665 110.875 3.713 46.115 1.00 14.42 D ATOM 8638 NZ LYS D 665 109.447 3.311 45.873 1.00 17.38 D ATOM 8639 C LYS D 665 113.202 −1.149 46.868 1.00 15.50 D ATOM 8640 O LYS D 665 112.216 −1.709 46.413 1.00 18.21 D ATOM 8641 N PHE D 666 114.352 −1.778 47.069 1.00 15.94 D ATOM 8642 CA PHE D 666 114.492 −3.207 46.810 1.00 16.38 D ATOM 8643 CB PHE D 666 114.453 −3.531 45.291 1.00 12.81 D ATOM 8644 CG PHE D 666 115.613 −2.980 44.477 1.00 13.72 D ATOM 8645 CD1 PHE D 666 116.914 −3.428 44.676 1.00 14.32 D ATOM 8646 CD2 PHE D 666 115.386 −2.051 43.460 1.00 16.32 D ATOM 8647 CE1 PHE D 666 117.963 −2.962 43.881 1.00 12.43 D ATOM 8648 CE2 PEE D 666 116.433 −1.579 42.659 1.00 14.70 D ATOM 8649 CZ PHE D 666 117.716 −2.039 42.873 1.00 15.14 D ATOM 8650 C PHE D 666 115.764 −3.767 47.482 1.00 17.88 D ATOM 8651 O PHE D 666 116.618 −3.017 47.971 1.00 18.62 D ATOM 8652 N SER D 667 115.869 −5.088 47.533 1.00 19.07 D ATOM 8653 CA SER D 667 117.021 −5.736 48.127 1.00 20.16 D ATOM 8654 CE SER D 667 116.971 −5.646 49.661 1.00 21.18 D ATOM 8655 OG SER D 667 115.778 −6.192 50.188 1.00 21.36 D ATOM 8656 C SER D 667 117.089 −7.188 47.675 1.00 19.78 D ATOM 8657 O SER D 667 116.093 −7.907 47.662 1.00 18.38 D ATOM 8658 N TYR D 668 118.280 −7.596 47.274 1.00 20.33 D ATOM 8659 CA TYR D 668 118.499 −8.946 46.807 1.00 21.29 D ATOM 8660 CE TYR D 668 118.756 −8.936 45.293 1.00 21.18 D ATOM 8661 CG TYR D 668 117.595 −8.369 44.470 1.00 20.55 D ATOM 8662 CD1 TYR D 668 116.495 −9.171 44.114 1.00 18.14 D ATOM 8663 CE1 TYR D 668 115.423 −8.647 43.403 1.00 18.24 D ATOM 8664 CD2 TYR D 668 117.584 −7.020 44.084 1.00 18.54 D ATOM 8665 CE2 TYR D 668 116.522 −6.484 43.379 1.00 18.25 D ATOM 8666 CZ TYR D 668 115.437 −7.293 43.044 1.00 19.79 D ATOM 8667 OH TYR D 668 114.343 −6.732 42.410 1.00 18.58 D ATOM 8668 C TYR D 668 119.709 −9.445 47.560 1.00 21.68 D ATOM 8669 O TYR D 668 120.525 −8.650 48.008 1.00 24.28 D ATOM 8670 N HIS D 669 119.802 −10.757 47.718 1.00 23.30 D ATOM 8671 CA HIS D 669 120.904 −11.398 48.413 1.00 23.12 D ATOM 8672 CB HIS D 669 120.433 −11.895 49.771 1.00 23.33 D ATOM 8673 CG HIS D 669 121.343 −11.528 50.897 1.00 26.89 D ATOM 8674 CD2 HIS D 669 121.187 −10.654 51.921 1.00 25.28 D ATOM 8675 ND1 HIS D 669 122.608 −12.060 51.034 1.00 26.65 D ATOM 8676 CE1 HIS D 669 123.193 −11.529 52.093 1.00 27.24 D ATOM 8677 NE2 HIS D 669 122.353 −10.673 52.649 1.00 27.53 D ATOM 8678 C HIS D 669 121.274 −12.587 47.535 1.00 24.51 D ATOM 8679 O HIS D 669 120.399 −13.313 47.036 1.00 24.95 D ATOM 8680 N HIS D 670 122.569 −12.779 47.335 1.00 24.99 D ATOM 8681 CA HIS D 670 123.045 −13.882 46.521 1.00 25.59 D ATOM 8682 CE HIS D 670 124.501 −13.642 46.121 1.00 26.37 D ATOM 8683 CG HIS D 670 124.666 −12.905 44.823 1.00 29.01 D ATOM 8684 CD2 HIS D 670 125.637 −12.971 43.881 1.00 27.78 D ATOM 8685 ND1 HIS D 670 123.779 −11.942 44.387 1.00 28.88 D ATOM 8686 CE1 HIS D 670 124.199 −11.450 43.236 1.00 26.47 D ATOM 8687 NE2 HIS D 670 125.324 −12.055 42.907 1.00 25.99 D ATOM 8688 C HIS D 670 122.918 −15.176 47.326 1.00 27.14 D ATOM 8689 O HIS D 670 123.583 −15.346 48.362 1.00 25.08 D ATOM 8690 N THR D 671 122.059 −16.080 46.840 1.00 28.13 D ATOM 8691 CA THR D 671 121.796 −17.381 47.473 1.00 27.79 D ATOM 8692 CB THR D 671 121.180 −18.369 46.454 1.00 26.12 D ATOM 8693 OG1 THR D 671 119.789 −18.069 46.289 1.00 23.95 D ATOM 8694 CG2 THR D 671 121.312 −19.791 46.930 1.00 26.83 D ATOM 8695 C THR D 671 122.992 −18.034 48.162 1.00 29.31 D ATOM 8696 O THR D 671 122.854 −18.547 49.271 1.00 29.25 D ATOM 8697 N ASN D 672 124.156 −18.025 47.516 1.00 31.23 D ATOM 8698 CA ASN D 672 125.354 −18.627 48.116 1.00 33.42 D ATOM 8699 CB ASN D 672 126.498 −18.738 47.089 1.00 35.89 D ATOM 8700 CG ASN D 672 126.323 −19.911 46.105 1.00 40.95 D ATOM 8701 OD1 ASN D 672 125.241 −20.116 45.535 1.00 42.75 D ATOM 8702 ND2 ASN D 672 127.406 −20.672 45.887 1.00 42.55 D ATOM 8703 C ASN D 672 125.861 −17.813 49.317 1.00 33.48 D ATOM 8704 O ASN D 672 126.666 −18.302 50.105 1.00 35.72 D ATOM 8705 N LEU D 673 125.405 −16.574 49.455 1.00 31.40 D ATOM 8706 CA LEU D 673 125.864 −15.722 50.549 1.00 30.75 D ATOM 8707 CB LEU D 673 125.631 −16.410 51.901 1.00 30.83 D ATOM 8708 CG LEU D 673 124.165 −16.514 52.344 1.00 31.99 D ATOM 8709 CD1 LEU D 673 124.059 −17.284 53.649 1.00 32.25 D ATOM 8710 CD2 LEU D 673 123.580 −15.115 52.510 1.00 33.43 D ATOM 8711 C LEU D 673 127.346 −15.337 50.420 1.00 28.49 D ATOM 8712 O LEU D 673 128.045 −15.214 51.429 1.00 29.31 D ATOM 8713 N SER D 674 127.812 −15.145 49.185 1.00 24.89 D ATOM 8714 CA SER D 674 129.201 −14.771 48.911 1.00 23.72 D ATOM 8715 CB SER D 674 129.764 −15.608 47.764 1.00 23.54 D ATOM 8716 OG SER D 674 128.969 −15.454 46.598 1.00 27.66 D ATOM 8717 C SER D 674 129.289 −13.287 48.546 1.00 22.55 D ATOM 8718 O SER D 674 128.336 −12.721 48.035 1.00 22.93 D ATOM 8719 N ALA D 675 130.431 −12.657 48.796 1.00 21.17 D ATOM 8720 CA ALA D 675 130.580 −11.240 48.498 1.00 20.35 D ATOM 8721 CB ALA D 675 132.002 −10.779 48.814 1.00 16.29 D ATOM 8722 C ALA D 675 130.215 −10.836 47.075 1.00 20.97 D ATOM 8723 O ALA D 675 130.528 −11.527 46.095 1.00 22.46 D ATOM 8724 N ILE D 676 129.538 −9.703 46.972 1.00 21.38 D ATOM 8725 CA ILE D 676 129.180 −9.194 45.667 1.00 23.44 D ATOM 8726 CB ILE D 676 128.051 −8.132 45.734 1.00 24.56 D ATOM 8727 CG2 ILE D 676 127.897 −7.484 44.377 1.00 23.13 D ATOM 8728 CG1 ILE D 676 126.727 −8.776 46.197 1.00 25.69 D ATOM 8729 CD1 ILE D 676 126.316 −10.018 45.386 1.00 25.28 D ATOM 8730 C ILE D 676 130.470 −8.526 45.202 1.00 23.09 D ATOM 8731 O ILE D 676 130.971 −7.613 45.853 1.00 23.97 D ATOM 8732 N THR D 677 131.012 −9.000 44.091 1.00 21.72 D ATOM 8733 CA THR D 677 132.250 −8.474 43.554 1.00 21.86 D ATOM 8734 CB THR D 677 133.096 −9.589 42.896 1.00 25.37 D ATOM 8735 OG1 THR D 677 133.515 −10.542 43.884 1.00 25.75 D ATOM 8736 CG2 THR D 677 134.328 −8.977 42.219 1.00 27.86 D ATOM 8737 C THR D 677 132.001 −7.420 42.488 1.00 20.83 D ATOM 8738 O THR D 677 132.880 −6.605 42.208 1.00 17.53 D ATOM 8739 N THR D 678 130.818 −7.457 41.876 1.00 20.52 D ATOM 8740 CA THR D 678 130.492 −6.512 40.821 1.00 19.25 D ATOM 8741 CB THR D 678 131.294 −6.864 39.512 1.00 20.24 D ATOM 8742 OG1 THR D 678 131.093 −5.842 38.533 1.00 19.49 D ATOM 8743 CG2 THR D 678 130.834 −8.193 38.927 1.00 17.27 D ATOM 8744 C THR D 678 129.001 −6.490 40.495 1.00 18.40 D ATOM 8745 O THR D 678 128.308 −7.497 40.627 1.00 17.73 D ATOM 8746 N PHE D 679 128.521 −5.336 40.044 1.00 19.50 D ATOM 8747 CA PHE D 679 127.119 −5.179 39.653 1.00 20.10 D ATOM 8748 CB PHE D 679 126.212 −5.151 40.896 1.00 19.62 D ATOM 8749 CG PHE D 679 126.072 −3.794 41.546 1.00 20.58 D ATOM 8750 CD1 PHE D 679 125.187 −2.838 41.036 1.00 19.81 D ATOM 8751 CD2 PHE D 679 126.786 −3.493 42.708 1.00 22.11 D ATOM 8752 CE1 PHE D 679 125.008 −1.595 41.679 1.00 19.56 D ATOM 8753 CE2 PHE D 679 126.622 −2.255 43.369 1.00 21.42 D ATOM 8754 CZ PHE D 679 125.730 −1.305 42.855 1.00 20.49 D ATOM 8755 C PHE D 679 126.967 −3.908 38.836 1.00 18.56 D ATOM 8756 O PHE D 679 127.824 −3.040 38.902 1.00 18.64 D ATOM 8757 N TYR D 680 125.900 −3.826 38.038 1.00 18.73 D ATOM 8758 CA TYR D 680 125.610 −2.640 37.216 1.00 18.62 D ATOM 8759 CB TYR D 680 126.140 −2.818 35.776 1.00 19.64 D ATOM 8760 CG TYR D 680 126.416 −1.498 35.070 1.00 21.94 D ATOM 8761 CD1 TYR D 680 127.503 −0.704 35.447 1.00 21.42 D ATOM 8762 CE1 TYR D 680 127.691 0.578 34.917 1.00 21.58 D ATOM 8763 CD2 TYR D 680 125.525 −0.982 34.123 1.00 21.80 D ATOM 8764 CE2 TYR D 680 125.702 0.304 33.585 1.00 21.45 D ATOM 8765 CZ TYR D 680 126.780 1.083 33.992 1.00 21.61 D ATOM 8766 OH TYR D 680 126.891 2.384 33.541 1.00 21.38 D ATOM 8767 C TYR D 680 124.087 −2.429 37.194 1.00 18.89 D ATOM 8768 O TYR D 680 123.326 −3.394 37.244 1.00 21.29 D ATOM 8769 N VAL D 681 123.635 −1.182 37.148 1.00 18.55 D ATOM 8770 CA VAL D 681 122.202 −0.952 37.112 1.00 20.06 D ATOM 8771 CB VAL D 681 121.588 −0.612 38.502 1.00 19.46 D ATOM 8772 CG1 VAL D 681 121.748 −1.770 39.427 1.00 23.82 D ATOM 8773 CG2 VAL D 681 122.219 0.634 39.080 1.00 18.66 D ATOM 8774 C VAL D 681 121.699 0.134 36.196 1.00 21.12 D ATOM 8775 O VAL D 681 122.429 1.030 35.748 1.00 19.50 D ATOM 8776 N SER D 682 120.404 0.039 35.956 1.00 22.21 D ATOM 8777 CA SER D 682 119.698 0.991 35.147 1.00 21.87 D ATOM 8778 CB SER D 682 119.633 0.520 33.703 1.00 20.44 D ATOM 8779 OG SER D 682 118.589 −0.410 33.525 1.00 21.95 D ATOM 8780 C SER D 682 118.331 0.950 35.783 1.00 23.11 D ATOM 8781 O SER D 682 118.048 0.053 36.582 1.00 22.65 D ATOM 8782 N ASP D 683 117.483 1.910 35.457 1.00 23.07 D ATOM 8783 CA ASP D 683 116.165 1.901 36.050 1.00 23.72 D ATOM 8784 CB ASP D 683 115.359 3.107 35.591 1.00 26.85 D ATOM 8785 CG ASP D 683 115.822 4.384 36.224 1.00 30.20 D ATOM 8786 OD1 ASP D 683 116.151 4.341 37.431 1.00 35.54 D ATOM 8787 OD2 ASP D 683 115.840 5.421 35.521 1.00 28.97 D ATOM 8788 C ASP D 683 115.381 0.631 35.728 1.00 22.90 D ATOM 8789 O ASP D 683 114.466 0.281 36.458 1.00 22.58 D ATOM 8790 N ASN D 684 115.717 −0.072 34.653 1.00 21.68 D ATOM 8791 CA ASN D 684 114.937 −1.257 34.335 1.00 21.96 D ATOM 8792 CB ASN D 684 114.568 −1.291 32.842 1.00 20.91 D ATOM 8793 CG ASN D 684 113.639 −0.138 32.417 1.00 22.88 D ATOM 8794 OD1 ASN D 684 112.685 0.229 33.132 1.00 20.08 D ATOM 8795 ND2 ASN D 684 113.907 0.423 31.231 1.00 21.27 D ATOM 8796 C ASN D 684 115.561 −2.597 34.705 1.00 22.28 D ATOM 8797 O ASN D 684 114.840 −3.557 34.983 1.00 21.62 D ATOM 8798 N ILE D 685 116.890 −2.659 34.735 1.00 22.22 D ATOM 8799 CA ILE D 685 117.592 −3.906 35.022 1.00 24.26 D ATOM 8800 CB ILE D 685 118.241 −4.431 33.725 1.00 25.72 D ATOM 8801 CG2 ILE D 685 119.014 −5.722 33.987 1.00 28.28 D ATOM 8802 CG1 ILE D 685 117.181 −4.607 32.646 1.00 26.62 D ATOM 8803 CD1 ILE D 685 117.527 −3.851 31.344 1.00 32.32 D ATOM 8804 C ILE D 685 118.701 −3.830 36.081 1.00 25.44 D ATOM 8805 O ILE D 685 119.291 −2.771 36.300 1.00 25.75 D ATOM 8806 N LEU D 686 118.989 −4.964 36.717 1.00 25.66 D ATOM 8807 CA LEU D 686 120.069 −5.041 37.689 1.00 26.90 D ATOM 8808 CB LEU D 686 119.530 −5.089 39.127 1.00 26.08 D ATOM 8809 CG LEU D 686 120.472 −5.572 40.262 1.00 23.99 D ATOM 8810 CD1 LEU D 686 121.709 −4.699 40.345 1.00 23.40 D ATOM 8811 CD2 LEU D 686 119.740 −5.567 41.585 1.00 21.28 D ATOM 8812 C LEU D 686 120.859 −6.317 37.412 1.00 28.01 D ATOM 8813 O LEU D 686 120.275 −7.397 37.340 1.00 28.42 D ATOM 8814 N VAL D 687 122.170 −6.194 37.226 1.00 26.81 D ATOM 8815 CA VAL D 687 122.995 −7.371 37.019 1.00 28.16 D ATOM 8816 CB VAL D 687 123.648 −7.401 35.629 1.00 28.88 D ATOM 8817 CG1 VAL D 687 124.496 −8.669 35.484 1.00 27.76 D ATOM 8818 CG2 VAL D 687 122.562 −7.383 34.553 1.00 29.55 D ATOM 8819 C VAL D 687 124.064 −7.347 38.098 1.00 29.32 D ATOM 8820 O VAL D 687 124.744 −6.331 38.291 1.00 29.09 D ATOM 8821 N SER D 688 124.200 −8.465 38.813 1.00 28.34 D ATOM 8822 CA SER D 688 125.166 −8.570 39.910 1.00 27.42 D ATOM 8823 CB SER D 688 124.419 −8.567 41.247 1.00 26.52 D ATOM 8824 OG SER D 688 123.505 −9.651 41.304 1.00 25.52 D ATOM 8825 C SER D 688 125.990 −9.853 39.808 1.00 27.67 D ATOM 8826 O SER D 688 125.518 −10.870 39.304 1.00 28.15 D ATOM 8827 N GLY D 689 127.217 −9.818 40.299 1.00 25.88 D ATOM 8828 CA GLY D 689 128.012 −11.016 40.228 1.00 25.97 D ATOM 8829 C GLY D 689 128.901 −11.218 41.422 1.00 27.10 D ATOM 8830 O GLY D 689 129.549 −10.285 41.890 1.00 29.72 D ATOM 8831 N SER D 690 128.914 −12.445 41.922 1.00 27.15 D ATOM 8832 CA SER D 690 129.752 −12.819 43.042 1.00 27.45 D ATOM 8833 CB SER D 690 128.918 −13.015 44.300 1.00 26.48 D ATOM 8834 OG SER D 690 127.975 −14.044 44.099 1.00 25.71 D ATOM 8835 C SER D 690 130.376 −14.145 42.630 1.00 28.76 D ATOM 8836 O SER D 690 130.435 −14.457 41.444 1.00 28.74 D ATOM 8837 N GLU D 691 130.829 −14.925 43.609 1.00 29.69 D ATOM 8838 CA GLU D 691 131.446 −16.210 43.320 1.00 29.80 D ATOM 8839 CB GLU D 691 132.241 −16.711 44.532 1.00 30.89 D ATOM 8840 CG GLU D 691 132.740 −18.153 44.426 1.00 34.76 D ATOM 8841 CD GLU D 691 133.806 −18.516 45.469 1.00 37.18 D ATOM 8842 OE1 GLU D 691 134.895 −17.901 45.448 1.00 39.22 D ATOM 8843 OE2 GLU D 691 133.564 −19.420 46.305 1.00 38.14 D ATOM 8844 C GLD D 691 130.409 −17.239 42.888 1.00 29.94 D ATOM 8845 O GLU D 691 129.441 −17.507 43.596 1.00 28.81 D ATOM 8846 N ASN D 692 130.621 −17.784 41.693 1.00 30.68 D ATOM 8847 CA ASN D 692 129.756 −18.800 41.122 1.00 30.63 D ATOM 8848 CB ASN D 692 129.854 −20.070 41.975 1.00 32.82 D ATOM 8849 CG ASN D 692 131.019 −20.951 41.562 1.00 34.81 D ATOM 8850 OD1 ASN D 692 130.832 −21.908 40.812 1.00 39.00 D ATOM 8851 ND2 ASN D 692 132.231 −20.614 42.016 1.00 34.40 D ATOM 8852 C ASN D 692 128.313 −18.370 40.941 1.00 30.73 D ATOM 8853 O ASN D 692 127.395 −19.187 40.996 1.00 31.82 D ATOM 8854 N GLN D 693 128.113 −17.081 40.711 1.00 30.83 D ATOM 8855 CA GLN D 693 126.774 −16.564 40.496 1.00 30.85 D ATOM 8856 CB GLN D 693 126.127 −16.215 41.837 1.00 32.95 D ATOM 8857 CG GLN D 693 125.494 −17.398 42.562 1.00 36.48 D ATOM 8858 CD CLN D 693 124.636 −16.949 43.741 1.00 39.48 D ATOM 8859 OE1 GLN D 693 123.650 −16.222 43.571 1.00 40.51 D ATOM 8860 NE2 GLN D 693 125.014 −17.371 44.941 1.00 40.67 D ATOM 8861 C GLN D 693 126.771 −15.350 39.560 1.00 30.20 D ATOM 8862 O GLN D 693 127.694 −14.533 39.586 1.00 28.95 D ATOM 8863 N PHE D 694 125.729 −15.268 38.728 1.00 28.92 D ATOM 8864 CA PHE D 694 125.534 −14.189 37.758 1.00 27.46 D ATOM 8865 CB PHE D 694 126.183 −14.549 36.404 1.00 26.85 D ATOM 8866 CG PHE D 694 126.212 −13.402 35.413 1.00 27.99 D ATOM 8867 CD1 PHE D 694 127.027 −12.290 35.626 1.00 28.31 D ATOM 8868 CD2 PHE D 694 125.387 −13.411 34.291 1.00 28.25 D ATOM 8869 CE1 PHE D 694 127.011 −11.201 34.734 1.00 25.87 D ATOM 8870 CE2 PHE D 694 125.365 −12.329 33.397 1.00 26.35 D ATOM 8871 CZ PHE D 694 126.175 −11.226 33.620 1.00 24.43 D ATOM 8872 C PHE D 694 124.018 −14.020 37.600 1.00 26.65 D ATOM 8873 O PHE D 694 123.360 −14.804 36.923 1.00 27.90 D ATOM 8874 N ASN D 695 123.462 −12.997 38.235 1.00 25.11 D ATOM 8875 CA ASN D 695 122.033 −12.784 38.169 1.00 22.66 D ATOM 8876 CE ASN D 695 121.462 −12.735 39.570 1.00 21.74 D ATOM 8877 CG ASN D 695 121.802 −13.948 40.351 1.00 22.53 D ATOM 8878 OD1 ASN D 695 122.469 −13.863 41.381 1.00 25.44 D ATOM 8879 ND2 ASN D 695 121.369 −15.102 39.866 1.00 21.60 D ATOM 8880 C ASN D 695 121.586 −11.557 37.431 1.00 22.56 D ATOM 8881 O ASN D 695 122.283 −10.537 37.402 1.00 24.25 D ATOM 8882 N ILE D 696 120.407 −11.675 36.828 1.00 20.27 D ATOM 8883 CA ILE D 696 119.785 −10.570 36.112 1.00 18.17 D ATOM 8884 CB ILE D 696 119.741 −10.848 34.598 1.00 13.96 D ATOM 8885 CG2 ILE D 696 119.173 −9.631 33.874 1.00 12.40 D ATOM 8886 CG1 ILE D 696 121.165 −11.096 34.095 1.00 11.96 D ATOM 8887 CD1 ILE D 696 121.278 −11.411 32.627 1.00 10.15 D ATOM 8888 C ILE D 696 118.375 −10.387 36.708 1.00 19.43 D ATOM 8889 O ILE D 696 117.558 −11.307 36.714 1.00 19.49 D ATOM 8890 N TYR D 697 118.130 −9.194 37.236 1.00 18.77 D ATOM 8891 CA TYR D 697 116.878 −8.867 37.881 1.00 17.94 D ATOM 8892 CB TYR D 697 117.167 −8.295 39.280 1.00 19.60 D ATOM 8893 CG TYR D 697 118.014 −9.185 40.171 1.00 19.57 D ATOM 8894 CD1 TYR D 697 117.428 −10.186 40.962 1.00 20.99 D ATOM 8895 CE1 TYR D 697 118.204 −11.012 41.789 1.00 18.57 D ATOM 8896 CD2 TYR D 697 119.397 −9.031 40.223 1.00 18.67 D ATOM 8897 CE2 TYR D 697 120.179 −9.840 41.035 1.00 19.21 D ATOM 8898 CZ TYR D 697 119.581 −10.832 41.820 1.00 20.43 D ATOM 8899 OH TYR D 697 120.372 −11.634 42.627 1.00 20.44 D ATOM 8900 C TYR D 697 116.059 −7.843 37.104 1.00 18.57 D ATOM 8901 O TYR D 697 116.604 −6.934 36.456 1.00 18.53 D ATOM 8902 N ASN D 698 114.746 −7.975 37.208 1.00 16.25 D ATOM 8903 CA ASN D 698 113.826 −7.049 36.575 1.00 16.13 D ATOM 8904 CB ASN D 698 112.594 −7.832 36.111 1.00 16.70 D ATOM 8905 CG ASN D 698 111.516 −6.939 35.508 1.00 18.93 D ATOM 8906 OD1 ASN D 698 111.253 −5.822 36.004 1.00 16.72 D ATOM 8907 ND2 ASN D 698 110.873 −7.428 34.443 1.00 16.48 D ATOM 8908 C ASN D 698 113.441 −6.032 37.682 1.00 15.83 D ATOM 8909 O ASN D 698 112.568 −6.301 38.499 1.00 14.84 D ATOM 8910 N LEU D 699 114.078 −4.874 37.735 1.00 14.22 D ATOM 8911 CA LEU D 699 113.725 −3.948 38.796 1.00 15.47 D ATOM 8912 CB LEU D 699 114.549 −2.673 38.704 1.00 11.67 D ATOM 8913 CG LEU D 699 115.818 −2.596 39.541 1.00 12.58 D ATOM 8914 CD LEU D 699 116.357 −4.000 39.957 1.00 9.17 D ATOM 8915 CD2 LEU D 699 116.822 −1.809 38.724 1.00 9.81 D ATOM 8916 C LEU D 699 112.260 −3.560 38.883 1.00 18.10 D ATOM 8917 O LEU D 699 111.836 −3.053 39.914 1.00 21.11 D ATOM 8918 N ARG D 700 111.479 −3.765 37.826 1.00 19.06 D ATOM 8919 CA ARG D 700 110.063 −3.382 37.889 1.00 18.41 D ATOM 8920 CB ARG D 700 109.474 −3.190 36.481 1.00 16.13 D ATOM 8921 CG ARG D 700 110.078 −2.053 35.660 1.00 18.32 D ATOM 8922 CD ARG D 700 109.605 −2.100 34.188 1.00 19.47 D ATOM 8923 NE ARG D 700 110.340 −1.195 33.295 1.00 19.60 D ATOM 8924 CZ ARG D 700 109.881 −0.738 32.127 1.00 20.84 D ATOM 8925 NH1 ARG D 700 108.678 −1.085 31.693 1.00 19.16 D ATOM 8926 NH2 ARG D 700 110.633 0.057 31.378 1.00 20.52 D ATOM 8927 C ARG D 700 109.211 −4.411 38.652 1.00 19.19 D ATOM 8928 O ARG D 700 108.440 −4.069 39.546 1.00 20.01 D ATOM 8929 N SER D 701 109.344 −5.673 38.286 1.00 18.61 D ATOM 8930 CA SER D 701 108.580 −6.719 38.919 1.00 18.99 D ATOM 8931 CB SER D 701 108.403 −7.907 37.960 1.00 17.26 D ATOM 8932 OG SER D 701 109.627 −8.299 37.350 1.00 16.41 D ATOM 8933 C SER D 701 109.317 −7.179 40.154 1.00 21.34 D ATOM 8934 O SER D 701 108.758 −7.881 40.983 1.00 21.67 D ATOM 8935 N GLY D 702 110.577 −6.782 40.277 1.00 23.17 D ATOM 8936 CA GLY D 702 111.367 −7.189 41.420 1.00 25.46 D ATOM 8937 C GLY D 702 111.916 −8.601 41.338 1.00 26.82 D ATOM 8938 O GLY D 702 112.676 −9.008 42.208 1.00 28.70 D ATOM 8939 N LYS D 703 111.580 −9.346 40.290 1.00 28.39 D ATOM 8940 CA LYS D 703 112.040 −10.734 40.187 1.00 29.97 D ATOM 8941 CE LYS D 703 110.926 −11.616 39.609 1.00 30.86 D ATOM 8942 CG LYS D 703 109.566 −11.294 40.211 1.00 34.24 D ATOM 8943 CD LYS D 703 108.553 −12.393 40.031 1.00 36.04 D ATOM 8944 CE LYS D 703 108.971 −13.657 40.786 1.00 38.38 D ATOM 8945 NZ LYS D 703 107.900 −14.711 40.780 1.00 39.62 D ATOM 8946 C LYS D 703 113.319 −11.022 39.428 1.00 30.16 D ATOM 8947 O LYS D 703 113.822 −10.202 38.665 1.00 33.16 D ATOM 8948 N LEU D 704 113.824 −12.227 39.655 1.00 31.22 D ATOM 8949 CA LEU D 704 115.037 −12.717 39.024 1.00 31.13 D ATOM 8950 CE LEU D 704 115.655 −13.799 39.894 1.00 28.59 D ATOM 8951 CG LEU D 704 116.959 −14.425 39.433 1.00 29.39 D ATOM 8952 CD1 LEU D 704 118.092 −13.385 39.446 1.00 31.25 D ATOM 8953 CD2 LEU D 704 117.298 −15.548 40.368 1.00 27.62 D ATOM 8954 C LEU D 704 114.663 −13.302 37.668 1.00 32.42 D ATOM 8955 O LEU D 704 113.791 −14.167 37.585 1.00 34.11 D ATOM 8956 N VAL D 705 115.308 −12.827 36.607 1.00 32.96 D ATOM 8957 CA VAL D 705 115.014 −13.329 35.275 1.00 33.27 D ATOM 8958 CB VAL D 705 115.052 −12.240 34.214 1.00 31.84 D ATOM 8959 CG1 VAL D 705 114.710 −12.853 32.866 1.00 33.49 D ATOM 8960 CG2 VAL D 705 114.079 −11.142 34.544 1.00 30.65 D ATOM 8961 C VAL D 705 116.011 −14.389 34.841 1.00 35.05 D ATOM 8962 O VAL D 705 115.632 −15.501 34.504 1.00 37.11 D ATOM 8963 N HIS D 706 117.291 −14.041 34.827 1.00 36.45 D ATOM 8964 CA HIS D 706 118.316 −14.991 34.426 1.00 36.74 D ATOM 8965 CB HIS D 706 119.007 −14.539 33.137 1.00 37.71 D ATOM 8966 CG HIS D 706 118.064 −14.142 32.042 1.00 40.20 D ATOM 8967 CD2 HIS D 706 117.901 −12.964 31.392 1.00 41.01 D ATOM 8968 ND1 HIS D 706 117.172 −15.022 31.468 1.00 40.45 D ATOM 8969 CE1 HIS D 706 116.504 −14.404 30.509 1.00 41.40 D ATOM 8970 NE2 HIS D 706 116.927 −13.155 30.441 1.00 41.00 D ATOM 8971 C HIS D 706 119.361 −15.155 35.527 1.00 37.89 D ATOM 8972 O HIS D 706 119.869 −14.174 36.096 1.00 38.65 D ATOM 8973 N ALA D 707 119.686 −16.414 35.805 1.00 37.80 D ATOM 8974 CA ALA D 707 120.660 −16.757 36.828 1.00 36.66 D ATOM 8975 CB ALA D 707 119.935 −17.223 38.075 1.00 33.53 D ATOM 8976 C ALA D 707 121.651 −17.828 36.367 1.00 36.44 D ATOM 8977 O ALA D 707 122.608 −18.138 37.079 1.00 36.66 D ATOM 8978 N ASN D 708 121.446 −18.382 35.177 1.00 36.37 D ATOM 8979 CA ASN D 708 122.347 −19.431 34.710 1.00 37.18 D ATOM 8980 CB ASN D 708 121.553 −20.739 34.521 1.00 37.73 D ATOM 8981 CG ASN D 708 120.893 −21.212 35.821 1.00 38.57 D ATOM 8982 OD1 ASN D 708 119.667 −21.227 35.947 1.00 38.35 D ATOM 8983 ND2 ASN D 708 121.712 −21.588 36.794 1.00 37.37 D ATOM 8984 C ASN D 708 123.137 −19.084 33.443 1.00 36.59 D ATOM 8985 O ASN D 708 123.856 −19.927 32.907 1.00 35.29 D ATOM 8986 N ILE D 709 123.019 −17.839 32.986 1.00 35.82 D ATOM 8987 CA ILE D 709 123.709 −17.402 31.781 1.00 34.43 D ATOM 8988 CB ILE D 709 123.349 −15.928 31.408 1.00 32.34 D ATOM 8989 CG2 ILE D 709 124.151 −15.460 30.221 1.00 30.43 D ATOM 8990 CG1 ILE D 709 121.875 −15.836 31.017 1.00 30.65 D ATOM 8991 CD1 ILE D 709 121.444 −14.459 30.565 1.00 28.79 D ATOM 8992 C ILE D 709 125.216 −17.552 31.873 1.00 34.88 D ATOM 8993 O ILE D 709 125.863 −17.878 30.882 1.00 36.86 D ATOM 8994 N LEU D 710 125.785 −17.336 33.051 1.00 34.63 D ATOM 8995 CA LEU D 710 127.232 −17.454 33.186 1.00 32.46 D ATOM 8996 CB LEU D 710 127.837 −16.058 33.402 1.00 28.39 D ATOM 8997 CG LEU D 710 128.450 −15.306 32.208 1.00 25.87 D ATOM 8998 CD1 LEU D 710 127.798 −15.707 30.894 1.00 24.33 D ATOM 8999 CD2 LEU D 710 128.331 −13.810 32.443 1.00 23.04 D ATOM 9000 C LEU D 710 127.683 −18.434 34.269 1.00 33.52 D ATOM 9001 O LEU D 710 128.730 −18.246 34.882 1.00 34.43 D ATOM 9002 N LYS D 711 126.902 −19.494 34.480 1.00 34.36 D ATOM 9003 CA LYS D 711 127.230 −20.518 35.481 1.00 35.44 D ATOM 9004 CB LYS D 711 126.238 −21.670 35.389 1.00 34.96 D ATOM 9005 CG LYS D 711 125.872 −22.006 33.980 1.00 36.79 D ATOM 9006 CD LYS D 711 124.620 −22.834 33.940 1.00 38.39 D ATOM 9007 CE LYS D 711 124.936 −24.285 34.192 1.00 40.21 D ATOM 9008 NZ LYS D 711 125.841 −24.794 33.104 1.00 42.27 D ATOM 9009 C LYS D 711 128.645 −21.068 35.350 1.00 36.53 D ATOM 9010 O LYS D 711 129.284 −21.427 36.341 1.00 36.63 D ATOM 9011 N ASP D 712 129.130 −21.126 34.121 1.00 37.64 D ATOM 9012 CA ASP D 712 130.457 −21.629 33.836 1.00 39.74 D ATOM 9013 CB ASP D 712 130.688 −21.555 32.336 1.00 44.17 D ATOM 9014 CG ASP D 712 129.490 −22.032 31.558 1.00 49.91 D ATOM 9015 OD1 ASP D 712 129.338 −23.276 31.408 1.00 53.21 D ATOM 9016 OD2 ASP D 712 128.684 −21.163 31.122 1.00 51.40 D ATOM 9017 C ASP D 712 131.548 −20.856 34.551 1.00 39.02 D ATOM 9018 O ASP D 712 132.528 −21.439 34.992 1.00 39.79 D ATOM 9019 N ALA D 713 131.398 −19.542 34.647 1.00 37.44 D ATOM 9020 CA ALA D 713 132.427 −18.740 35.295 1.00 37.31 D ATOM 9021 CB ALA D 713 132.131 −17.254 35.119 1.00 37.40 D ATOM 9022 C ALA D 713 132.603 −19.055 36.775 1.00 36.89 D ATOM 9023 O ALA D 713 131.693 −19.535 37.437 1.00 37.66 D ATOM 9024 N ASP D 714 133.785 −18.782 37.296 1.00 35.36 D ATOM 9025 CA ASP D 714 134.018 −19.033 38.693 1.00 34.87 D ATOM 9026 CB ASP D 714 135.384 −19.678 38.893 1.00 33.94 D ATOM 9027 CG ASP D 714 135.484 −21.038 38.244 1.00 32.23 D ATOM 9028 OD1 ASP D 714 134.599 −21.877 38.477 1.00 32.51 D ATOM 9029 OD2 ASP D 714 136.456 −21.279 37.505 1.00 34.54 D ATOM 9030 C ASP D 714 133.946 −17.705 39.433 1.00 35.72 D ATOM 9031 O ASP D 714 133.610 −17.651 40.616 1.00 35.20 D ATOM 9032 N GLN D 715 134.238 −16.629 38.714 1.00 35.93 D ATOM 9033 CA GLN D 715 134.233 −15.293 39.284 1.00 36.18 D ATOM 9034 CE GLN D 715 135.648 −14.938 39.750 1.00 37.10 D ATOM 9035 CG GLN D 715 136.260 −15.951 40.716 1.00 39.05 D ATOM 9036 CD GLN D 715 135.897 −15.672 42.165 1.00 40.12 D ATOM 9037 OE1 GLN D 715 134.751 −15.380 42.472 1.00 42.68 D ATOM 9038 NE2 GLN D 715 136.874 −15.763 43.057 1.00 39.97 D ATOM 9039 C GLN D 715 133.756 −14.264 38.254 1.00 35.81 D ATOM 9040 O GLN D 715 133.993 −14.407 37.054 1.00 35.76 D ATOM 9041 N ILE D 716 133.073 −13.232 38.736 1.00 34.56 D ATOM 9042 CA ILE D 716 132.582 −12.149 37.888 1.00 32.51 D ATOM 9043 CB ILE D 716 131.061 −11.982 38.032 1.00 31.79 D ATOM 9044 CG2 ILE D 716 130.547 −11.006 36.996 1.00 30.49 D ATOM 9045 CG1 ILE D 716 130.363 −13.336 37.890 1.00 33.24 D ATOM 9046 CD1 ILE D 716 130.638 −14.060 36.579 1.00 34.30 D ATOM 9047 C ILE D 716 133.285 −10.863 38.375 1.00 32.59 D ATOM 9048 O ILE D 716 132.797 −10.160 39.264 1.00 33.77 D ATOM 9049 N TRP D 717 134.444 −10.580 37.795 1.00 30.84 D ATOM 9050 CA TRP D 717 135.252 −9.429 38.162 1.00 29.11 D ATOM 9051 CE TRP D 717 136.558 −9.454 37.379 1.00 32.71 D ATOM 9052 CG TRP D 717 137.348 −10.687 37.596 1.00 35.43 D ATOM 9053 CD2 TRP D 717 137.669 −11.278 38.855 1.00 35.53 D ATOM 9054 CE2 TRP D 717 138.462 −12.416 38.589 1.00 36.83 D ATOM 9055 CE3 TRP D 717 137.364 −10.960 40.185 1.00 35.83 D ATOM 9056 CD1 TRP D 717 137.940 −11.464 36.640 1.00 36.35 D ATOM 9057 NE1 TRP D 717 138.612 −12.504 37.230 1.00 37.07 D ATOM 9058 CZ2 TRP D 717 138.956 −13.237 39.605 1.00 38.32 D ATOM 9059 CZ3 TRP D 717 137.855 −11.780 41.193 1.00 37.12 D ATOM 9060 CH2 TRP D 717 138.641 −12.904 40.896 1.00 37.38 D ATOM 9061 C TRP D 717 134.583 −8.102 37.930 1.00 26.79 D ATOM 9062 O TRP D 717 134.507 −7.262 38.825 1.00 24.62 D ATOM 9063 N SER D 718 134.110 −7.899 36.713 1.00 24.96 D ATOM 9064 CA SER D 718 133.473 −6.639 36.403 1.00 23.33 D ATOM 9065 CB SER D 718 134.499 −5.674 35.830 1.00 21.39 D ATOM 9066 OG SER D 718 133.898 −4.420 35.620 1.00 24.14 D ATOM 9067 C SER D 718 132.347 −6.825 35.421 1.00 22.63 D ATOM 9068 O SER D 718 132.481 −7.549 34.443 1.00 25.60 D ATOM 9069 N VAL D 719 131.228 −6.175 35.679 1.00 21.31 D ATOM 9070 CA VAL D 719 130.095 −6.286 34.784 1.00 23.17 D ATOM 9071 CB VAL D 719 128.900 −6.926 35.517 1.00 23.18 D ATOM 9072 CG1 VAL D 719 128.244 −5.916 36.483 1.00 23.48 D ATOM 9073 CG2 VAL D 719 127.915 −7.427 34.517 1.00 24.77 D ATOM 9074 C VAL D 719 129.703 −4.887 34.255 1.00 24.78 D ATOM 9075 O VAL D 719 130.024 −3.864 34.872 1.00 25.63 D ATOM 9076 N ASN D 720 129.005 −4.835 33.125 1.00 25.17 D ATOM 9077 CA ASN D 720 128.604 −3.547 32.543 1.00 25.66 D ATOM 9078 CB ASN D 720 129.844 −2.787 31.999 1.00 25.58 D ATOM 9079 CG ASN D 720 129.627 −1.256 31.853 1.00 26.08 D ATOM 9080 OD1 ASN D 720 128.697 −0.790 31.193 1.00 24.37 D ATOM 9081 ND2 ASN D 720 130.527 −0.484 32.456 1.00 24.14 D ATOM 9082 C ASN D 720 127.665 −3.882 31.397 1.00 25.69 D ATOM 9083 O ASN D 720 127.961 −4.770 30.601 1.00 24.75 D ATOM 9084 N PHE D 721 126.524 −3.209 31.324 1.00 25.70 D ATOM 9085 CA PHE D 721 125.610 −3.473 30.226 1.00 25.92 D ATOM 9086 CB PHE D 721 124.486 −4.426 30.663 1.00 24.85 D ATOM 9087 CG PHE D 721 123.483 −3.803 31.566 1.00 23.85 D ATOM 9088 CD1 PHE D 721 122.441 −3.052 31.043 1.00 22.92 D ATOM 9089 CD2 PHE D 721 123.588 −3.938 32.941 1.00 22.57 D ATOM 9090 CE1 PHE D 721 121.525 −2.442 31.877 1.00 21.91 D ATOM 9091 CE2 PHE D 721 122.675 −3.328 33.777 1.00 22.55 D ATOM 9092 CZ PHE D 721 121.640 −2.579 33.243 1.00 21.48 D ATOM 9093 C PHE D 721 125.076 −2.145 29.706 1.00 26.21 D ATOM 9094 O PHE D 721 125.149 −1.120 30.402 1.00 25.17 D ATOM 9095 N LYS D 722 124.564 −2.166 28.473 1.00 26.41 D ATOM 9096 CA LYS D 722 124.046 −0.966 27.801 1.00 25.77 D ATOM 9097 CB LYS D 722 125.230 −0.140 27.287 1.00 25.66 D ATOM 9098 CG LYS D 722 125.220 1.340 27.627 1.00 26.55 D ATOM 9099 CD LYS D 722 124.193 2.106 26.828 1.00 28.07 D ATOM 9100 CE LYS D 722 124.609 3.586 26.571 1.00 31.04 D ATOM 9101 NZ LYS D 722 125.623 3.789 25.462 1.00 31.59 D ATOM 9102 C LYS D 722 123.152 −1.376 26.621 1.00 25.54 D ATOM 9103 O LYS D 722 123.556 −2.161 25.765 1.00 24.73 D ATOM 9104 N GLY D 723 121.936 −0.851 26.580 1.00 25.69 D ATOM 9105 CA GLY D 723 121.044 −1.201 25.497 1.00 25.26 D ATOM 9106 C GLY D 723 120.804 −2.694 25.431 1.00 27.03 D ATOM 9107 O GLY D 723 120.226 −3.287 26.342 1.00 28.21 D ATOM 9108 N LYS D 724 121.262 −3.313 24.350 1.00 28.66 D ATOM 9109 CA LYS D 724 121.087 −4.752 24.144 1.00 29.79 D ATOM 9110 CB LYS D 724 120.590 −4.978 22.732 1.00 30.45 D ATOM 9111 CG LYS D 724 121.344 −4.146 21.713 1.00 32.48 D ATOM 9112 CD LYS D 724 122.379 −4.944 20.947 1.00 34.54 D ATOM 9113 CE LYS D 724 122.796 −4.163 19.693 1.00 36.42 D ATOM 9114 NZ LYS D 724 123.789 −4.878 18.817 1.00 36.97 D ATOM 9115 C LYS D 724 122.373 −5.535 24.346 1.00 29.03 D ATOM 9116 O LYS D 724 122.417 −6.749 24.142 1.00 28.40 D ATOM 9117 N THR D 725 123.409 −4.820 24.759 1.00 28.23 D ATOM 9118 CA THR D 725 124.720 −5.400 24.964 1.00 27.95 D ATOM 9119 CB THR D 725 125.784 −4.578 24.178 1.00 27.43 D ATOM 9120 OG1 THR D 725 125.351 −4.417 22.821 1.00 26.72 D ATOM 9121 CG2 THR D 725 127.134 −5.273 24.189 1.00 25.82 D ATOM 9122 C THR D 725 125.106 −5.460 26.443 1.00 27.90 D ATOM 9123 O THR D 725 124.891 −4.505 27.199 1.00 28.70 D ATOM 9124 N LEU D 726 125.682 −6.591 26.842 1.00 26.83 D ATOM 9125 CA LEU D 726 126.119 −6.806 28.213 1.00 24.94 D ATOM 9126 CB LEU D 726 125.126 −7.703 28.937 1.00 27.71 D ATOM 9127 CG LEU D 726 125.632 −8.393 30.211 1.00 29.98 D ATOM 9128 CD1 LEU D 726 126.114 −7.390 31.271 1.00 30.93 D ATOM 9129 CD2 LEU D 726 124.478 −9.202 30.758 1.00 31.05 D ATOM 9130 C LEU D 726 127.485 −7.441 28.245 1.00 22.94 D ATOM 9131 O LEU D 726 127.673 −8.537 27.741 1.00 24.07 D ATOM 9132 N VAL D 727 128.436 −6.753 28.856 1.00 23.62 D ATOM 9133 CA VAL D 727 129.798 −7.256 28.940 1.00 23.62 D ATOM 9134 CB VAL D 727 130.766 −6.218 28.377 1.00 24.57 D ATOM 9135 CG1 VAL D 727 132.189 −6.737 28.490 1.00 28.26 D ATOM 9136 CG2 VAL D 727 130.414 −5.939 26.896 1.00 22.22 D ATOM 9137 C VAL D 727 130.214 −7.625 30.360 1.00 21.59 D ATOM 9138 O VAL D 727 129.738 −7.034 31.333 1.00 20.77 D ATOM 9139 N ALA D 728 131.106 −8.608 30.461 1.00 21.47 D ATOM 9140 CA ALA D 728 131.597 −9.084 31.751 1.00 21.74 D ATOM 9141 CB ALA D 728 130.593 −10.057 32.371 1.00 23.07 D ATOM 9142 C ALA D 728 132.952 −9.749 31.692 1.00 21.99 D ATOM 9143 O ALA D 728 133.199 −10.624 30.846 1.00 17.98 D ATOM 9144 N ALA D 729 133.823 −9.315 32.605 1.00 24.10 D ATOM 9145 CA ALA D 729 135.175 −9.868 32.740 1.00 25.79 D ATOM 9146 CB ALA D 729 136.139 −8.792 33.225 1.00 26.49 D ATOM 9147 C ALA D 729 135.036 −10.980 33.770 1.00 26.20 D ATOM 9148 O ALA D 729 134.619 −10.736 34.900 1.00 24.79 D ATOM 9149 N VAL D 730 135.363 −12.199 33.351 1.00 27.91 D ATOM 9150 CA VAL D 730 135.224 −13.396 34.182 1.00 28.52 D ATOM 9151 CB VAL D 730 134.162 −14.349 33.578 1.00 25.65 D ATOM 9152 CD1 VAL D 730 132.846 −13.619 33.401 1.00 21.69 D ATOM 9153 CD2 VAL D 730 134.667 −14.910 32.251 1.00 23.86 D ATOM 9154 C VAL D 730 136.496 −14.215 34.373 1.00 30.60 D ATOM 9155 O VAL D 730 137.544 −13.945 33.773 1.00 29.25 D ATOM 9156 N GLU D 731 136.373 −15.227 35.224 1.00 34.05 D ATOM 9157 CA GLU D 731 137.468 −16.136 35.507 1.00 38.43 D ATOM 9158 CB GLU D 731 138.069 −15.875 36.877 1.00 39.08 D ATOM 9159 CG GLU D 731 139.163 −16.851 37.195 1.00 41.06 D ATOM 9160 CD GLU D 731 139.469 −16.908 38.664 1.00 44.19 D ATOM 9161 OE1 GLU D 731 139.986 −15.898 39.204 1.00 43.94 D ATOM 9162 OE2 GLU D 731 139.184 −17.969 39.275 1.00 45.15 D ATOM 9163 C GLU D 731 136.915 −17.541 35.481 1.00 39.52 D ATOM 9164 O GLU D 731 136.003 −17.862 36.239 1.00 38.90 D ATOM 9165 N LYS D 732 137.464 −18.375 34.606 1.00 42.02 D ATOM 9166 CA LYS D 732 137.000 −19.744 34.487 1.00 44.14 D ATOM 9167 CB LYS D 732 136.079 −19.864 33.279 1.00 45.79 D ATOM 9168 CG LYS D 732 135.263 −21.130 33.269 1.00 48.52 D ATOM 9169 CD LYS D 732 134.329 −21.169 32.074 1.00 48.95 D ATOM 9170 CE LYS D 732 133.753 −22.555 31.897 1.00 50.73 D ATOM 9171 NZ LYS D 732 132.777 −22.576 30.795 1.00 53.14 D ATOM 9172 C LYS D 732 138.155 −20.724 34.366 1.00 45.13 D ATOM 9173 O LYS D 732 139.012 −20.593 33.491 1.00 46.00 D ATOM 9174 N ASP D 733 138.179 −21.702 35.263 1.00 45.68 D ATOM 9175 CA ASP D 733 139.227 −22.710 35.263 1.00 45.99 D ATOM 9176 CE ASP D 733 139.114 −23.590 34.013 1.00 47.96 D ATOM 9177 CG ASP D 733 137.759 −24.322 33.917 1.00 51.97 D ATOM 9178 OD1 ASP D 733 137.355 −24.977 34.905 1.00 55.70 D ATOM 9179 OD2 ASP D 733 137.095 −24.256 32.855 1.00 50.55 D ATOM 9180 C ASP D 733 140.603 −22.066 35.311 1.00 45.97 D ATOM 9181 O ASP D 733 141.493 −22.456 34.565 1.00 46.45 D ATOM 9182 N GLY D 734 140.778 −21.075 36.182 1.00 45.60 D ATOM 9183 CA GLY D 734 142.072 −20.420 36.295 1.00 44.79 D ATOM 9184 C GLY D 734 142.438 −19.447 35.182 1.00 44.98 D ATOM 9185 O GLY D 734 143.607 −19.089 35.012 1.00 44.45 D ATOM 9186 N GLN D 735 141.453 −19.010 34.411 1.00 43.41 D ATOM 9187 CA GLN D 735 141.747 −18.067 33.349 1.00 42.41 D ATOM 9188 CB GLN D 735 141.935 −18.820 32.034 1.00 44.33 D ATOM 9189 CG GLN D 735 143.185 −19.679 32.036 1.00 46.62 D ATOM 9190 CD GLN D 735 143.303 −20.555 30.810 1.00 48.33 D ATOM 9191 OE1 GLN D 735 143.228 −20.076 29.670 1.00 49.33 D ATOM 9192 NE2 GLN D 735 143.495 −21.853 31.035 1.00 48.62 D ATOM 9193 C GLN D 735 140.647 −17.025 33.243 1.00 40.32 D ATOM 9194 O GLN D 735 139.504 −17.282 33.609 1.00 40.35 D ATOM 9195 N SER D 736 141.001 −15.841 32.765 1.00 37.70 D ATOM 9196 CA SER D 736 140.033 −14.770 32.630 1.00 35.67 D ATOM 9197 CB SER D 736 140.664 −13.454 33.051 1.00 35.55 D ATOM 9198 OG SER D 736 141.815 −13.209 32.262 1.00 33.28 D ATOM 9199 C SER D 736 139.580 −14.656 31.191 1.00 35.08 D ATOM 9200 O SER D 736 140.375 −14.823 30.273 1.00 35.01 D ATOM 9201 N PHE D 737 138.299 −14.370 30.998 1.00 35.00 D ATOM 9202 CA PHE D 737 137.749 −14.215 29.662 1.00 34.26 D ATOM 9203 CB PHE D 737 136.928 −15.436 29.259 1.00 34.41 D ATOM 9204 CG PHE D 737 137.736 −16.689 29.121 1.00 34.85 D ATOM 9205 CD1 PHE D 737 138.122 −17.416 30.243 1.00 34.24 D ATOM 9206 CD2 PHE D 737 138.120 −17.140 27.864 1.00 34.84 D ATOM 9207 CE1 PHE D 737 138.871 −18.574 30.108 1.00 34.16 D ATOM 9208 CE2 PHE D 737 138.868 −18.293 27.724 1.00 33.97 D ATOM 9209 CZ PHE D 737 139.246 −19.012 28.845 1.00 34.14 D ATOM 9210 C PHE D 737 136.869 −12.992 29.611 1.00 33.97 D ATOM 9211 O PHE D 737 136.627 −12.359 30.639 1.00 34.16 D ATOM 9212 N LEU D 738 136.387 −12.673 28.411 1.00 32.98 D ATOM 9213 CA LEU D 738 135.526 −11.514 28.199 1.00 33.21 D ATOM 9214 CB LEU D 738 136.222 −10.527 27.255 1.00 32.13 D ATOM 9215 CG LEU D 738 135.744 −9.075 27.237 1.00 32.97 D ATOM 9216 CD1 LEU D 738 134.465 −8.962 26.461 1.00 33.24 D ATOM 9217 CD2 LEU D 738 135.574 −8.569 28.668 1.00 33.16 D ATOM 9218 C LEU D 738 134.180 −11.955 27.620 1.00 33.76 D ATOM 9219 O LEU D 738 134.110 −12.360 26.473 1.00 36.66 D ATOM 9220 N GLU D 739 133.114 −11.870 28.410 1.00 33.64 D ATOM 9221 CA GLU D 739 131.793 −12.292 27.959 1.00 32.51 D ATOM 9222 CB GLU D 739 131.000 −12.884 29.121 1.00 33.25 D ATOM 9223 CG GLU D 739 131.529 −14.166 29.668 1.00 34.95 D ATOM 9224 CD GLU D 739 131.644 −15.235 28.602 1.00 38.68 D ATOM 9225 OE1 GLU D 739 130.731 −15.323 27.733 1.00 38.32 D ATOM 9226 OE2 GLU D 739 132.651 −15.991 28.646 1.00 39.63 D ATOM 9227 C GLU D 739 130.961 −11.163 27.377 1.00 32.88 D ATOM 9228 O GLU D 739 130.735 −10.144 28.044 1.00 33.94 D ATOM 9229 N ILE D 740 130.487 −11.329 26.147 1.00 31.70 D ATOM 9230 CA ILE D 740 129.641 −10.301 25.568 1.00 29.64 D ATOM 9231 CB ILE D 740 130.288 −9.670 24.299 1.00 28.27 D ATOM 9232 CG2 ILE D 740 129.461 −8.484 23.831 1.00 27.08 D ATOM 9233 CG1 ILE D 740 131.663 −9.093 24.620 1.00 24.97 D ATOM 9234 CD1 ILE D 740 132.282 −8.385 23.424 1.00 24.47 D ATOM 9235 C ILE D 740 128.275 −10.906 25.252 1.00 29.65 D ATOM 9236 O ILE D 740 128.174 −11.845 24.470 1.00 30.71 D ATOM 9237 N LEU D 741 127.226 −10.388 25.885 1.00 30.03 D ATOM 9238 CA LEU D 741 125.872 −10.903 25.659 1.00 30.25 D ATOM 9239 CB LEU D 741 125.209 −11.213 26.994 1.00 30.19 D ATOM 9240 CG LEU D 741 126.016 −12.176 27.872 1.00 30.17 D ATOM 9241 CD1 LEU D 741 125.458 −12.120 29.284 1.00 31.69 D ATOM 9242 CD2 LEU D 741 125.969 −13.591 27.323 1.00 26.90 D ATOM 9243 C LEU D 741 125.012 −9.935 24.863 1.00 29.80 D ATOM 9244 O LEU D 741 124.939 −8.750 25.176 1.00 28.77 D ATOM 9245 N ASP D 742 124.354 −10.462 23.837 1.00 31.56 D ATOM 9246 CA ASP D 742 123.513 −9.664 22.948 1.00 32.74 D ATOM 9247 CB ASP D 742 123.917 −9.906 21.492 1.00 33.83 D ATOM 9248 CG ASP D 742 123.601 −8.730 20.592 1.00 34.30 D ATOM 9249 OD1 ASP D 742 122.422 −8.315 20.526 1.00 33.76 D ATOM 9250 OD2 ASP D 742 124.550 −8.223 19.952 1.00 34.48 D ATOM 9251 C ASP D 742 122.046 −10.021 23.110 1.00 33.39 D ATOM 9252 O ASP D 742 121.617 −11.102 22.713 1.00 33.45 D ATOM 9253 N PHE D 743 121.283 −9.097 23.685 1.00 34.50 D ATOM 9254 CA PHE D 743 119.858 −9.296 23.905 1.00 34.56 D ATOM 9255 CB PHE D 743 119.422 −8.544 25.161 1.00 32.05 D ATOM 9256 CG PHE D 743 119.627 −9.324 26.400 1.00 29.59 D ATOM 9257 CD1 PHE D 743 120.893 −9.462 26.941 1.00 27.43 D ATOM 9258 CD2 PHE D 743 118.579 −10.058 26.935 1.00 28.98 D ATOM 9259 CE1 PHE D 743 121.116 −10.332 27.987 1.00 26.97 D ATOM 9260 CE2 PHE D 743 118.787 −10.933 27.980 1.00 27.93 D ATOM 9261 CZ PHE D 743 120.059 −11.077 28.507 1.00 26.94 D ATOM 9262 C PHE D 743 118.973 −8.895 22.734 1.00 35.12 D ATOM 9263 O PHE D 743 117.746 −8.889 22.849 1.00 35.80 D ATOM 9264 N SER D 744 119.594 −8.592 21.600 1.00 35.35 D ATOM 9265 CA SER D 744 118.854 −8.176 20.416 1.00 35.76 D ATOM 9266 CB SER D 744 119.823 −7.612 19.381 1.00 36.40 D ATOM 9267 OG SER D 744 119.126 −6.857 18.417 1.00 40.54 D ATOM 9268 C SER D 744 118.029 −9.301 19.793 1.00 35.75 D ATOM 9269 O SER D 744 118.433 −10.488 19.873 1.00 36.28 D ATOM 9270 OXT SER D 744 116.984 −8.972 19.209 1.00 34.82 D ATOM 9271 CB LEU E 2 57.203 −3.013 76.696 1.00 93.40 E ATOM 9272 CG LEU E 2 56.802 −2.909 78.154 1.00 92.64 E ATOM 9273 CD1 LEU E 2 56.089 −4.209 78.494 1.00 92.62 E ATOM 9274 CD2 LEU E 2 58.002 −2.716 79.063 1.00 91.70 E ATOM 9275 C LEU E 2 58.910 −2.837 74.950 1.00 94.06 E ATOM 9276 O LEU E 2 59.052 −4.056 75.064 1.00 94.80 E ATOM 9277 N LEU E 2 57.498 −0.813 75.549 1.00 93.79 E ATOM 9278 CA LEU E 2 58.180 −2.054 76.029 1.00 93.74 E ATOM 9279 N LEU E 3 59.349 −2.162 73.890 1.00 93.32 E ATOM 9280 CA LEU E 3 60.093 −2.853 72.840 1.00 91.84 E ATOM 9281 CS LEU E 3 60.099 −2.030 71.539 1.00 90.21 E ATOM 9282 CG LEU E 3 58.738 −2.011 70.818 1.00 88.51 E ATOM 9283 CD1 LEU E 3 58.863 −1.419 69.431 1.00 86.61 E ATOM 9284 CD2 LEU E 3 58.194 −3.426 70.729 1.00 87.78 E ATOM 9285 C LEU E 3 61.504 −3.132 73.355 1.00 91.93 E ATOM 9286 O LEU E 3 62.459 −2.428 73.011 1.00 92.22 E ATOM 9287 N TPO E 4 61.634 −4.171 74.204 1.00 91.56 E ATOM 9288 CA TPO E 4 62.536 −4.975 75.032 1.00 90.52 E ATOM 9289 CE TPO E 4 62.853 −4.058 76.249 1.00 89.37 E ATOM 9290 CG2 TPO E 4 63.717 −4.740 77.314 1.00 89.39 E ATOM 9291 OG1 TPO E 4 63.546 −2.864 75.833 1.00 86.87 E ATOM 9292 P TPO E 4 65.016 −2.884 75.092 1.00 83.35 E ATOM 9293 O1P TPO E 4 64.849 −3.624 73.731 1.00 83.36 E ATOM 9294 O2P TPO E 4 66.088 −3.641 76.006 1.00 83.80 E ATOM 9295 O3P TPO E 4 65.359 −1.340 74.831 1.00 84.80 E ATOM 9296 C TPO E 4 61.804 −6.259 75.507 1.00 91.34 E ATOM 9297 O TPO E 4 60.467 −6.316 75.619 1.00 91.46 E ATOM 9298 N PRO E 5 63.256 −5.997 71.948 1.00 83.51 E ATOM 9299 CD PRO E 5 63.441 −4.606 71.529 1.00 83.14 E ATOM 9300 CA PRO E 5 63.931 −6.885 71.003 1.00 84.53 E ATOM 9301 CE PRO E 5 65.159 −6.089 70.575 1.00 83.61 E ATOM 9302 OG PRO E 5 64.831 −4.637 70.919 1.00 83.06 E ATOM 9303 C PRO E 5 64.316 −8.236 71.564 1.00 85.50 E ATOM 9304 O PRO E 5 64.916 −8.330 72.628 1.00 85.67 E ATOM 9305 N PRO E 6 63.969 −9.312 70.847 1.00 86.93 E ATOM 9306 CD PRO E 6 63.085 −9.303 69.669 1.00 87.22 E ATOM 9307 CA PRO E 6 64.267 −10.690 71.255 1.00 88.33 E ATOM 9308 CE PRO E 6 63.629 −11.522 70.149 1.00 87.80 E ATOM 9309 CG PRO E 6 62.478 −10.688 69.722 1.00 87.62 E ATOM 9310 C PRO E 6 65.765 −10.988 71.384 1.00 89.85 E ATOM 9311 O PRO E 6 66.575 −10.544 70.557 1.00 90.61 E ATOM 9312 N GLN E 7 66.126 −11.745 72.421 1.00 90.83 E ATOM 9313 CA GLN E 7 67.515 −12.125 72.626 1.00 91.45 E ATOM 9314 CE GLN E 7 68.006 −11.682 73.992 1.00 91.16 E ATOM 9315 CG GLN E 7 68.555 −10.282 73.957 1.00 91.12 E ATOM 9316 CD GLN E 7 69.842 −10.165 74.739 1.00 91.14 E ATOM 9317 OE1 GLN E 7 69.851 −10.287 75.975 1.00 92.25 E ATOM 9318 NB2 GLN E 7 70.950 −9.958 74.025 1.00 89.30 E ATOM 9319 C GLN E 7 67.666 −13.631 72.485 1.00 91.90 E ATOM 9320 0 GLN E 7 67.429 −14.383 73.431 1.00 92.11 E ATOM 9321 N SER E 8 68.051 −14.055 71.282 1.00 92.25 E ATOM 9322 CA SER E 8 68.235 −15.467 70.933 1.00 92.14 E ATOM 9323 CE SER E 8 67.113 −15.896 69.981 1.00 92.25 E ATOM 9324 OG SER E 8 66.978 −17.305 69.938 1.00 92.67 E ATOM 9325 C SER E 8 69.603 −15.640 70.258 1.00 92.02 E ATOM 9326 O SER E 8 70.638 −15.398 70.879 1.00 91.94 E ATOM 9327 N GLY E 9 69.602 −16.057 68.994 1.00 91.78 E ATOM 9328 CA GLY E 9 70.854 −16.235 68.277 1.00 91.39 E ATOM 9329 C GLY E 9 70.848 −15.537 66.928 1.00 91.23 E ATOM 9330 O GLY E 9 69.743 −15.212 66.445 1.00 90.99 E ATOM 9331 OXT GLY E 9 71.939 −15.322 66.346 1.00 90.21 E ATOM 9332 CE LEU F 2 137.489 −5.702 48.818 1.00 79.71 F ATOM 9333 CG LEU F 2 138.842 −5.743 49.546 1.00 80.18 F ATOM 9334 CD1 LEU F 2 139.667 −4.549 49.099 1.00 79.66 F ATOM 9335 CD2 LEU F 2 138.661 −5.730 51.075 1.00 78.72 F ATOM 9336 C LEU F 2 138.487 −6.493 46.630 1.00 78.95 F ATOM 9337 O LEU F 2 138.336 −7.720 46.632 1.00 77.64 F ATOM 9338 N LEU F 2 136.056 −5.715 46.790 1.00 79.28 F ATOM 9339 CA LEU F 2 137.454 −5.545 47.286 1.00 79.36 F ATOM 9340 N LEU F 3 139.520 −5.871 46.060 1.00 78.25 F ATOM 9341 CA LEU F 3 140.670 −6.502 45.403 1.00 76.54 F ATOM 9342 CB LEU F 3 140.433 −6.740 43.915 1.00 77.32 F ATOM 9343 CG LEU F 3 139.459 −7.802 43.429 1.00 78.88 F ATOM 9344 CD1 LEU F 3 138.100 −7.190 43.081 1.00 80.14 F ATOM 9345 CD2 LEU F 3 140.065 −8.449 42.204 1.00 78.71 F ATOM 9346 C LEU F 3 141.723 −5.415 45.530 1.00 75.20 F ATOM 9347 O LEU F 3 141.444 −4.264 45.195 1.00 75.82 F ATOM 9348 N TPO F 4 142.936 −5.746 46.012 1.00 72.87 F ATOM 9349 CA TPO F 4 144.008 −4.734 46.163 1.00 70.82 F ATOM 9350 CB TPO F 4 144.161 −4.534 47.709 1.00 68.53 F ATOM 9351 CG2 TPO F 4 145.393 −3.748 48.146 1.00 70.46 F ATOM 9352 OG1 TPO F 4 142.965 −3.903 48.203 1.00 65.51 F ATOM 9353 P TPO F 4 142.778 −2.260 48.081 1.00 60.19 F ATOM 9354 O1P TPO F 4 142.871 −1.889 46.565 1.00 64.16 F ATOM 9355 O2P TPO F 4 143.905 −1.501 48.889 1.00 62.63 F ATOM 9356 O3P TPO F 4 141.319 −1.975 48.672 1.00 64.49 F ATOM 9357 C TPO F 4 145.311 −5.244 45.579 1.00 70.94 F ATOM 9358 O TPO F 4 145.629 −6.541 45.562 1.00 71.31 F ATOM 9359 N PRO F 5 146.116 −4.278 45.081 1.00 71.04 F ATOM 9360 CD PRO F 5 145.651 −2.886 44.895 1.00 69.22 F ATOM 9361 CA PRO F 5 147.434 −4.439 44.468 1.00 71.37 F ATOM 9362 CB PRO F 5 147.722 −3.051 43.898 1.00 70.57 F ATOM 9363 CG PRO F 5 146.379 −2.473 43.673 1.00 68.58 F ATOM 9364 C PRO F 5 148.447 −4.823 45.533 1.00 72.63 F ATOM 9365 O PRO F 5 148.273 −4.524 46.709 1.00 72.26 F ATOM 9366 N PRO F 6 149.531 −5.484 45.133 1.00 74.58 F ATOM 9367 CD PRO F 6 149.883 −5.888 43.760 1.00 74.65 F ATOM 9368 CA PRO F 6 150.563 −5.898 46.087 1.00 76.44 F ATOM 9369 CB PRO F 6 151.636 −6.499 45.180 1.00 76.17 F ATOM 9370 CG PRO F 6 150.843 −7.015 44.005 1.00 75.36 F ATOM 9371 C PRO F 6 151.108 −4.721 46.907 1.00 78.12 F ATOM 9372 O PRO F 6 151.745 −3.827 46.351 1.00 78.87 F ATOM 9373 N GLN F 7 150.858 −4.699 48.213 1.00 79.62 F ATOM 9374 CA GLN F 7 151.397 −3.605 49.020 1.00 81.37 F ATOM 9375 CB GLN F 7 150.607 −3.435 50.333 1.00 81.68 F ATOM 9376 CG GLN F 7 151.014 −2.213 51.171 1.00 82.68 F ATOM 9377 CD GLN F 7 150.936 −0.896 50.397 1.00 83.36 F ATOM 9378 OE1 GLN F 7 151.562 −0.740 49.343 1.00 84.22 F ATOM 9379 NE2 GLN F 7 150.175 0.061 50.927 1.00 82.82 F ATOM 9380 C GLN F 7 152.866 −3.939 49.299 1.00 82.45 F ATOM 9381 O GLN F 7 153.186 −4.607 50.282 1.00 82.78 F ATOM 9382 N SER F 8 153.745 −3.472 48.411 1.00 83.82 F ATOM 9383 CA SER F 8 155.196 −3.704 48.479 1.00 85.47 F ATOM 9384 CB SER F 8 155.937 −2.583 47.732 1.00 84.24 F ATOM 9385 OG SER F 8 155.277 −2.236 46.527 1.00 83.28 F ATOM 9386 C SER F 8 155.813 −3.857 49.887 1.00 86.86 F ATOM 9387 O SER F 8 156.285 −2.881 50.482 1.00 87.36 F ATOM 9388 N GLY F 9 155.830 −5.093 50.390 1.00 87.52 F ATOM 9389 CA GLY F 9 156.387 −5.374 51.708 1.00 87.82 F ATOM 9390 C GLY F 9 155.445 −6.117 52.646 1.00 87.94 F ATOM 9391 O GLY F 9 154.243 −6.240 52.319 1.00 88.07 F ATOM 9392 OXT GLY F 9 155.901 −6.573 53.717 1.00 87.76 F END

[0525] TABLE 7 Oligonucleotides used in Example 2 MTO# Oligo name Sequence MTO 1146 LP6DelA-FWD gccttcgcgaactgatgtacactttgcagggtcatacagc MTO 1147 LP6DelA-REV gccttggccattttctagatcccaaattctaatagtggtatccatac MTO 1254 CDC4-BNSH-F gtaggatccatatgggcgccgcaagctttcccttagctgagtttcc MTO 1367 V384N-C catatgacgagtaatattacgtgcttgc MTO 1368 V384N3 caagcacgtaatattactcgtcatatg MTO 1369 K402A-C ggggctgatgacgcaatgatcagag MTO 1370 K402A-N ctctgatcattgcgtcatcagcccc MTO 1371 W426A 5′ gatggtggggttgcggcgctgaagtatgcccatg MTO 1372 DN426A catgggcatacttcagcgccgcaaccccaccatc MTO 1373 R443D-C ggttctacagacgacacggtccgagtttggg MTO 1374 R443D tatcccaaactcggaccgtgtcgtcgtctgtagaaccg MTO 1375 Y548F cagtgtattatcaaagcttccactaacgac MTO 1376 Y548F-C gtcgttagtggaagctttgataatacactg MTO 1377 Y574F-N gtagattgtcgaaaatattcgatccgtatg MTO 1378 Y574F-C catacggatcgaatattttcgacaatctac MTO 1379 W717N Hpa ttgcccttaaagttaaccgagttaatctgatcag MTO 1380 W717N-C ctgatcagattaactcggttaactttaagggcaa MTO 1381 2Flex359 5′ tcttttctggagcccgggccaattttaaaaaattggtac MTO 1382 2Flex359 3′ gtaccaattttttaaaattggcccgggctccagaaaaga MTO 1383 H5 Dest 5′ ggttttaattctctcggcccgggaccctcccaaaaatacccaaaactc MTO 1384 H5 Dest 3′ gagttttgggtatttttgggagggtcccgggccgagagaattaaaacc MTO 1385 H5 del 5′ gtgagcccaaagggtccaaagctttcacaacaagatcgc MTO 1386 H5 del 3′ gcgatcttgttgtgaaagctttggaccctttgggctcac MTO 1387 H5 + Dest 5′ gtggaaaaaacttctgatattcattttaaaaaattggtacaatcc MTO 1388 H5 + Dest 3′ ggattgtaccaattttttaaaatgaatatcagaagttttttccac MTO 1389 Ala1-3 ccaattttttaaaatgaatgcaatattctccagaaaag MTO 1390 Ala2-3 ccaattttttaaaatgaatgctgcaatattctccagaaaag MTO 1391 Ala3-3 ccaatttttttaaaatgaaagcggctgcaatattctccagaaaag MTO 1392 Ala4-3 ccaattttttaaaatgaaggctgcagctgcaatattctccagaaaag MTO 1393 Ala8 5′ gccgcgcgcgctaaagctgcagcgttcattttaaaaaattggtacaatcc MTO 1394 Ala8 3′ cgctgcagctttagcgcgcgcggctatattctccagaaaagataatc MTO 1395 Ala12 5′ gccgcgcgcgctaaagctgcagcgcgcgcgaaagccttcattttaaaaaattggtacaatcc MTO 1396 Al12 3′ ggctttcgcgcgcgctgcagctttagcgcgcgcggctatattctccagaaaagataatc

[0526] TABLE 8 Plasmids used in Example 2 Plasmid Relevant Characteristic Source pMT 3169 pProEx Hta-CDC4 LP6DelA GST-Skp1 This study pMT 3055 pProEx Hta-CDC4 263-744 GST-Skp1 Nash et. al. pMT 3000 pProEx Hta-CDC4 1-744 GST-Skp1 This study pMT 3217 pRS 314 CDC4-BNSH/Eco This study pMT 3001 pMT 3055 V384N This study pMT 3002 pMT 3055 K402A This study pMT 3385 pMT 3055 W426A This study pMT 3058 pMT 3055 R443A Nash et. al pMT 3003 pMT 3055 R443D This study pMT 3059 pMT 3055 R467A Nash et. al pMT 3060 pMT 3055 R485A Nash et. al pMT 3061 pMT 3055 R534A Nash et. al pMT 3004 pMT 3055 Y548F This study pMT 3005 pMT 3055 Y574F This study pMT 3006 pMT 3055 W717N This study pMT 3007 pMT 3055 V384N + W717N This study pMT 3008 pMT 3055 K402 + R443D This study pMT 3010 pMT 3000 R443D This study pMT 3011 pMT 3000 R443A This study pMT 3012 pMT 3000 W717N This study pMT 3013 pMT 3000 K402A + R443D This study pMT 3014 pMT 3000 V384N + W717N This study pMT 3015 pMT 3217 V384N This study pMT 3016 pMT 3217 K402A This study pMT 3386 pMT 3217 W426A This study pMT 3017 pMT 3217 R443D This study pMT 3058 PRS 314-CDC4 R443A Nash et. al. pMT 3018 pMT 3217 Y548F This study pMT 3068 PRS 314-CDC4 R572A Nash et. al pMT 3019 pMT 3217 Y574F This study pMT 3020 pMT 3217 W717N This study pMT 3021 pMT 3217 V384N + W717N This study pMT 3022 pMT 3217 K402A + R443D This study pMT 3024 pMT 3000 Helix 5 Δ 330-443 This study pMT 3025 pMT 3000 Helix 5 breaker This study pMT 3026 pMT 3000 Helix 5 Δ 321-360 This study pMT 3027 pMT 3000 Helix 6 breaker This study pMT 3028 pMT 3000 Ala1 insert This study pMT 3029 pMT 3000 Ala2 insert This study pMT 3030 pMT 3000 Ala3 insert This study pMT 3031 pMT 3000 Ala4 insert This study pMT 3032 pMT 3000 Ala8 insert This study pMT 3033 pMT 3000 Ala12 insert This study pMT 3034 pMT 3217 Helix 5 Δ 330-443 This study pMT 3035 pMT 3217 Helix 5 breaker This study pMT 3036 pMT 3217 Helix 5 Δ 321-360 This study pMT 3037 pMT 3217 Helix 6 breaker This study pMT 3038 pMT 3217 Ala1 insert This study pMT 3039 pMT 3217 Ala2 insert This study pMT 3040 pMT 3217 Ala3 insert This study pMT 3041 pMT 3217 Ala4 insert This study pMT 3042 pMT 3217 Ala8 insert This study pMT 3043 pMT 3217 Ala12 insert This study pMT 1571 Pet16b-Sic1 Previous study MDM 152 pGALl1 SIC1 LEU2 CEN ARS M. Mendenhall MDM202 pGAL1 SIC1^(T33V) LEU2 CEN ARS M. Mendenhall

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0 SEQUENCE LISTING <160> NUMBER OF SEQ ID NOS: 43 <210> SEQ ID NO 1 <211> LENGTH: 8 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (1)..(1) <223> OTHER INFORMATION: wherein Xaa can be either Ile or Leu <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (2)..(2) <223> OTHER INFORMATION: wherein Xaa can be either Ile, Leu or Pro <220> FEATURE: <221> NAME/KEY: MOD_RES <222> LOCATION: (3)..(3) <223> OTHER INFORMATION: PHOSPHORYLATION <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (5)..(5) <223> OTHER INFORMATION: wherein Xaa cannot be Lys or Arg <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (6)..(6) <223> OTHER INFORMATION: wherein Xaa cannot be Lys or Arg <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (7)..(7) <223> OTHER INFORMATION: wherein Xaa cannot be Lys or Arg <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (8)..(8) <223> OTHER INFORMATION: wherein Xaa cannot be Lys or Arg <400> SEQUENCE: 1 Xaa Xaa Thr Pro Xaa Xaa Xaa Xaa 1 5 <210> SEQ ID NO 2 <211> LENGTH: 4 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (1)..(1) <223> OTHER INFORMATION: wherin Xaa may be Ser or Thr <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (3)..(3) <223> OTHER INFORMATION: wherin Xaa can be any naturally occurring amino acid <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (4)..(4) <223> OTHER INFORMATION: wherin Xaa can be Lys or Arg <400> SEQUENCE: 2 Xaa Pro Xaa Xaa 1 <210> SEQ ID NO 3 <211> LENGTH: 194 <212> TYPE: PRT <213> ORGANISM: Saccharomyces cerevisiae <400> SEQUENCE: 3 Met Val Thr Ser Asn Val Val Leu Val Ser Gly Glu Gly Glu Arg Phe 1 5 10 15 Thr Val Asp Lys Lys Ile Ala Glu Arg Ser Leu Leu Leu Lys Asn Tyr 20 25 30 Leu Asn Asp Met His Asp Ser Asn Leu Gln Asn Asn Ser Asp Ser Glu 35 40 45 Ser Asp Ser Asp Ser Glu Thr Asn His Lys Ser Lys Asp Asn Asn Asn 50 55 60 Gly Asp Asp Asp Asp Glu Asp Asp Asp Glu Ile Val Met Pro Val Pro 65 70 75 80 Asn Val Arg Ser Ser Val Leu Gln Lys Val Ile Glu Trp Ala Glu His 85 90 95 His Arg Asp Ser Asn Phe Pro Asp Glu Asp Asp Asp Asp Ser Arg Lys 100 105 110 Ser Ala Pro Val Asp Ser Trp Asp Arg Glu Phe Leu Lys Val Asp Gln 115 120 125 Glu Met Leu Tyr Glu Ile Ile Leu Ala Ala Asn Tyr Leu Asn Ile Lys 130 135 140 Pro Leu Leu Asp Ala Gly Cys Lys Val Val Ala Glu Met Ile Arg Gly 145 150 155 160 Arg Ser Pro Glu Glu Ile Arg Arg Thr Phe Asn Ile Val Asn Asp Phe 165 170 175 Thr Pro Glu Glu Glu Ala Ala Ile Arg Arg Glu Asn Glu Trp Ala Glu 180 185 190 Asp Arg <210> SEQ ID NO 4 <211> LENGTH: 161 <212> TYPE: PRT <213> ORGANISM: Schizosaccharomyces pombe <400> SEQUENCE: 4 Met Ser Lys Ile Lys Leu Ile Ser Ser Asp Asn Glu Glu Phe Val Val 1 5 10 15 Asp Gln Leu Ile Ala Glu Arg Ser Met Leu Ile Lys Asn Met Leu Glu 20 25 30 Asp Val Gly Glu Ile Asn Val Pro Ile Pro Leu Pro Asn Val Ser Ser 35 40 45 Asn Val Leu Arg Lys Val Leu Glu Trp Cys Glu His His Lys Asn Asp 50 55 60 Leu Tyr Ser Gly Thr Glu Glu Glu Ser Asp Ile Arg Leu Lys Lys Ser 65 70 75 80 Thr Asp Ile Asp Glu Trp Asp Arg Lys Phe Met Ala Val Asp Gln Glu 85 90 95 Met Leu Phe Glu Ile Val Leu Ala Ser Asn Tyr Leu Asp Ile Lys Pro 100 105 110 Leu Leu Asp Thr Gly Cys Lys Thr Val Ala Asn Met Ile Arg Gly Lys 115 120 125 Ser Pro Glu Asp Ile Arg Lys Thr Phe Asn Ile Pro Asn Asp Phe Thr 130 135 140 Pro Glu Glu Glu Glu Gln Ile Arg Lys Glu Asn Glu Trp Ala Glu Asp 145 150 155 160 Arg <210> SEQ ID NO 5 <211> LENGTH: 165 <212> TYPE: PRT <213> ORGANISM: Caenorhabditis elegans <400> SEQUENCE: 5 Ala Lys Glu Arg Glu Ile Lys Ile Ser Ser Ser Asp Asn Glu Ile Phe 1 5 10 15 Leu Val Pro Arg Asn Val Ile Arg Leu Ser Asn Thr Ile Asn Thr Leu 20 25 30 Leu Met Asp Leu Gly Leu Asp Asp Glu Glu Gly Thr Asn Ala Glu Pro 35 40 45 Ile Pro Val Gln Asn Val Thr Ala Ser Ile Leu Lys Lys Val Ile Ser 50 55 60 Trp Cys Asn His His His Ser Asp Pro Ile Ser Thr Glu Asp Ser Asp 65 70 75 80 Asn Arg Glu Lys Arg Thr Asp Asp Ile Gly Ser Trp Asp Val Glu Phe 85 90 95 Leu Lys Val Asp Gln Gly Thr Leu Phe Glu Leu Ile Ala Ala Asn Tyr 100 105 110 Leu Asp Ile Lys Gly Leu Leu Asp Val Thr Cys Lys Thr Val Ala Asn 115 120 125 Met Ile Lys Gly Lys Ser Pro Glu Glu Ile Arg Arg Thr Phe Asn Ile 130 135 140 Lys Asn Asp Phe Thr Pro Glu Glu Glu Glu Gln Ile Arg Lys Glu Asn 145 150 155 160 Ala Trp Cys Glu Asp 165 <210> SEQ ID NO 6 <211> LENGTH: 162 <212> TYPE: PRT <213> ORGANISM: Drosophila melanogaster <400> SEQUENCE: 6 Met Pro Ser Ile Lys Leu Gln Ser Ser Asp Glu Glu Ile Phe Asp Thr 1 5 10 15 Asp Ile Gln Ile Ala Lys Cys Ser Gly Thr Ile Lys Thr Met Leu Glu 20 25 30 Asp Cys Gly Met Glu Asp Asp Glu Asn Ala Ile Val Pro Leu Pro Asn 35 40 45 Val Asn Ser Thr Ile Leu Arg Lys Val Leu Thr Trp Ala His Tyr His 50 55 60 Lys Asp Asp Pro Gln Pro Thr Glu Asp Asp Glu Ser Lys Glu Lys Arg 65 70 75 80 Thr Asp Asp Ile Ile Ser Trp Asp Ala Asp Phe Leu Lys Val Asp Gln 85 90 95 Gly Thr Leu Phe Glu Leu Ile Leu Ala Ala Asn Tyr Leu Asp Ile Lys 100 105 110 Gly Leu Leu Glu Leu Thr Cys Lys Thr Val Ala Asn Met Ile Lys Gly 115 120 125 Lys Thr Pro Glu Glu Ile Arg Lys Thr Phe Asn Ile Lys Lys Asp Phe 130 135 140 Ser Pro Ala Glu Glu Glu Gln Val Arg Lys Glu Asn Glu Trp Cys Glu 145 150 155 160 Glu Lys <210> SEQ ID NO 7 <211> LENGTH: 163 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <400> SEQUENCE: 7 Met Pro Ser Ile Lys Leu Gln Ser Ser Asp Gly Glu Ile Phe Glu Val 1 5 10 15 Asp Val Glu Ile Ala Lys Gln Ser Val Thr Ile Lys Thr Met Leu Glu 20 25 30 Asp Leu Gly Met Asp Asp Glu Gly Asp Asp Asp Pro Val Pro Leu Pro 35 40 45 Asn Val Asn Ala Ala Ile Leu Lys Lys Val Ile Gln Trp Cys Thr His 50 55 60 His Lys Asp Asp Pro Pro Pro Pro Glu Asp Asp Glu Asn Lys Glu Lys 65 70 75 80 Arg Thr Asp Asp Ile Pro Val Trp Asp Gln Glu Phe Leu Lys Val Asp 85 90 95 Gln Gly Thr Leu Phe Glu Leu Ile Leu Ala Ala Asn Tyr Leu Asp Ile 100 105 110 Lys Gly Leu Leu Asp Val Thr Cys Lys Thr Val Ala Asn Met Ile Lys 115 120 125 Gly Lys Thr Pro Glu Glu Ile Arg Lys Thr Phe Asn Ile Lys Asn Asp 130 135 140 Phe Thr Glu Glu Glu Glu Ala Gln Val Arg Lys Glu Asn Gln Trp Cys 145 150 155 160 Glu Glu Lys <210> SEQ ID NO 8 <211> LENGTH: 475 <212> TYPE: PRT <213> ORGANISM: Saccharomyces cerevisiae <400> SEQUENCE: 8 Leu Lys Arg Asp Leu Ile Thr Ser Leu Pro Phe Glu Ile Ser Leu Lys 1 5 10 15 Ile Phe Asn Tyr Leu Gln Phe Glu Asp Ile Ile Asn Ser Leu Gly Val 20 25 30 Ser Gln Asn Trp Asn Lys Ile Ile Arg Lys Ser Thr Ser Leu Trp Lys 35 40 45 Lys Leu Leu Ile Ser Glu Asn Phe Val Ser Pro Lys Gly Phe Asn Ser 50 55 60 Leu Asn Leu Lys Leu Ser Gln Lys Tyr Pro Lys Leu Ser Gln Gln Asp 65 70 75 80 Arg Leu Arg Leu Ser Phe Leu Glu Asn Ile Phe Ile Leu Lys Asn Trp 85 90 95 Tyr Asn Pro Lys Phe Val Pro Gln Arg Thr Thr Leu Arg Gly His Met 100 105 110 Thr Ser Val Ile Thr Cys Leu Gln Phe Glu Asp Asn Tyr Val Ile Thr 115 120 125 Gly Ala Asp Asp Lys Met Ile Arg Val Tyr Asp Ser Ile Asn Lys Lys 130 135 140 Phe Leu Leu Gln Leu Ser Gly His Asp Gly Gly Val Trp Ala Leu Lys 145 150 155 160 Tyr Ala His Gly Gly Ile Leu Val Ser Gly Ser Thr Asp Arg Thr Val 165 170 175 Arg Val Trp Asp Ile Lys Lys Gly Cys Cys Thr His Val Phe Lys Gly 180 185 190 His Asn Ser Thr Val Arg Cys Leu Asp Ile Val Glu Tyr Lys Asn Ile 195 200 205 Lys Tyr Ile Val Thr Gly Ser Arg Asp Asn Thr Leu His Val Trp Lys 210 215 220 Leu Pro Lys Glu Ser Ser Val Pro Asp His Gly Glu Glu His Asp Tyr 225 230 235 240 Pro Leu Val Phe His Thr Pro Glu Glu Asn Pro Tyr Phe Val Gly Val 245 250 255 Leu Arg Gly His Met Ala Ser Val Arg Thr Val Ser Gly His Gly Asn 260 265 270 Ile Val Val Ser Gly Ser Tyr Asp Asn Thr Leu Ile Val Trp Asp Val 275 280 285 Ala Gln Met Lys Cys Leu Tyr Ile Leu Ser Gly His Thr Asp Arg Ile 290 295 300 Tyr Ser Thr Ile Tyr Asp His Glu Arg Lys Arg Cys Ile Ser Ala Ser 305 310 315 320 Met Asp Thr Thr Ile Arg Ile Trp Asp Leu Glu Asn Ile Trp Asn Asn 325 330 335 Gly Glu Cys Ser Tyr Ala Thr Asn Ser Ala Ser Pro Cys Ala Lys Ile 340 345 350 Leu Gly Ala Met Tyr Thr Leu Gln Gly His Thr Ala Leu Val Gly Leu 355 360 365 Leu Arg Leu Ser Asp Lys Phe Leu Val Ser Ala Ala Ala Asp Gly Ser 370 375 380 Ile Arg Gly Trp Asp Ala Asn Asp Tyr Ser Arg Lys Phe Ser Tyr His 385 390 395 400 His Thr Asn Leu Ser Ala Ile Thr Thr Phe Tyr Val Ser Asp Asn Ile 405 410 415 Leu Val Ser Gly Ser Glu Asn Gln Phe Asn Ile Tyr Asn Leu Arg Ser 420 425 430 Gly Lys Leu Val His Ala Asn Ile Leu Lys Asp Ala Asp Gln Ile Trp 435 440 445 Ser Val Asn Phe Lys Gly Lys Thr Leu Val Ala Ala Val Glu Lys Asp 450 455 460 Gly Gln Ser Phe Leu Glu Ile Leu Asp Phe Ser 465 470 475 <210> SEQ ID NO 9 <211> LENGTH: 475 <212> TYPE: PRT <213> ORGANISM: Schizosaccharomyces pombe <400> SEQUENCE: 9 Phe Gln Lys Asn Phe Leu Thr Gly Phe Pro Ala Glu Ile Thr Asn Leu 1 5 10 15 Val Leu Thr His Leu Asp Ala Pro Ser Leu Cys Ala Val Ser Gln Val 20 25 30 Ser His His Trp Tyr Lys Leu Val Ser Ser Asn Glu Glu Leu Trp Lys 35 40 45 Ser Leu Phe Leu Lys Asp Gly Phe Phe Trp Asp Ser Ile Asp Ser Lys 50 55 60 Ile Arg Thr Met Cys Leu Glu Gln Ser Leu Ser Ala Cys Ala Ile Met 65 70 75 80 Lys Arg Val Tyr Phe Arg His Phe Asn Leu Arg Glu Arg Trp Leu His 85 90 95 Ala Pro Glu Lys Ile Lys Arg Cys Ser Phe Pro Ile His Gly Val Arg 100 105 110 Leu Ile Thr Lys Leu Gln Phe Asp Asp Asp Lys Ile Ile Val Ser Thr 115 120 125 Cys Ser Pro Arg Ile Asn Ile Tyr Asp Thr Lys Thr Gly Val Leu Ile 130 135 140 Arg Ser Leu Glu Glu His Glu Gly Asp Val Trp Thr Phe Glu Tyr Val 145 150 155 160 Gly Asp Thr Leu Val Thr Gly Ser Thr Asp Arg Thr Val Arg Val Trp 165 170 175 Asp Leu Arg Thr Gly Glu Cys Lys Gln Val Phe Tyr Gly His Thr Ser 180 185 190 Thr Ile Arg Cys Ile Lys Ile Val Gln Gly Asn Gln Ser Thr Thr Asp 195 200 205 Thr Asp Asp Val Glu Lys Glu Asn Arg Pro Ala Ser Asn Asp Ala Asn 210 215 220 Ser Met Pro Pro Tyr Ile Ile Ser Ser Ser Arg Asp Cys Thr Ile Arg 225 230 235 240 Leu Trp Ser Leu Pro Cys Leu Asp Asp Pro Pro Phe Val Asn Val Asn 245 250 255 Glu Asn Pro Asp Gln Asn Asn Asp Phe Thr Ser Ala Thr Thr Asn Pro 260 265 270 Phe Tyr Ile Arg Thr Leu Arg Gly His Thr Asp Ser Val Arg Glu Val 275 280 285 Ala Cys Leu Gly Asp Leu Ile Val Ser Ala Ser Tyr Asp Gly Thr Leu 290 295 300 Arg Val Trp Lys Ala Ser Thr Gly Val Cys Leu His Val Leu Arg Gly 305 310 315 320 His Val Gly Arg Val Tyr Ser Val Thr Ile Asn Pro Ser Arg Gln Gln 325 330 335 Cys Ile Ser Ala Gly Thr Asp Ala Lys Ile Arg Ile Trp Asn Leu Glu 340 345 350 Ser Gly Glu Leu Leu Gln Thr Leu His Gly His Ser Asn Leu Val Ser 355 360 365 Gln Val Thr Phe Asn Gln Asn Ile Leu Val Ser Ala Ser Ala Pro Pro 370 375 380 Asp Thr Ser Leu Arg Val Trp Asp Leu Asn Thr Gly Ser Cys Arg Asp 385 390 395 400 Ile Leu Lys Cys Pro Leu Gly His Ile Phe Phe Gln His Asp Glu Ser 405 410 415 Lys Val Val Ser Gly Ser His Ser Thr Leu Gln Leu Trp Asp Ile Arg 420 425 430 Ser Gly Lys Leu Val Arg Asp Leu Leu Thr Asp Leu Asp Ile Ile Trp 435 440 445 Gln Val Ala Tyr Asn Glu Asn Val Cys Val Ala Ala Val Leu Arg Asn 450 455 460 Asn Arg Phe Trp Ile Glu Val Leu Glu Phe Gly 465 470 475 <210> SEQ ID NO 10 <211> LENGTH: 465 <212> TYPE: PRT <213> ORGANISM: Caenorhabditis elegans <400> SEQUENCE: 10 Phe Gln Arg Asp Phe Leu Ser Cys Leu Pro Val Glu Leu Gly Met Lys 1 5 10 15 Ile Leu His Asn Leu Thr Gly Tyr Asp Leu Leu Lys Val Ala Gln Val 20 25 30 Ser Lys Asn Trp Lys Leu Ile Ser Glu Ile Asp Lys Ile Trp Lys Ser 35 40 45 Leu Gly Val Glu Glu Phe Lys His His Pro Asp Pro Thr Asp Arg Val 50 55 60 Thr Gly Ala Trp Gln Gly Thr Ala Ile Ala Ala Gly Val Thr Ile Pro 65 70 75 80 Asp His Ile Gln Pro Cys Asp Leu Asn Val His Arg Phe Leu Lys Leu 85 90 95 Gln Lys Phe Gly Asp Ile Phe Glu Arg Ala Ala Asp Lys Ser Arg Tyr 100 105 110 Leu Arg Ala Asp Lys Ile Glu Lys Asn Trp Asn Ala Asn Pro Ile Met 115 120 125 Gly Ser Ala Val Leu Arg Gly His Glu Asp His Val Ile Thr Cys Met 130 135 140 Gln Ile His Asp Asp Val Leu Val Thr Gly Ser Asp Asp Asn Thr Leu 145 150 155 160 Lys Val Trp Cys Ile Asp Lys Gly Glu Val Met Tyr Thr Leu Val Gly 165 170 175 His Thr Gly Gly Val Trp Thr Ser Gln Ile Ser Gln Cys Gly Arg Tyr 180 185 190 Ile Val Ser Gly Ser Thr Asp Arg Thr Val Lys Val Trp Ser Thr Val 195 200 205 Asp Gly Ser Leu Leu His Thr Leu Gln Gly His Thr Ser Thr Val Arg 210 215 220 Cys Met Ala Met Ala Gly Ser Ile Leu Val Thr Gly Ser Arg Asp Thr 225 230 235 240 Thr Leu Arg Val Trp Asp Val Glu Ser Gly Arg His Leu Ala Thr Leu 245 250 255 His Gly His His Ala Ala Val Arg Cys Val Gln Phe Asp Gly Thr Thr 260 265 270 Val Val Ser Gly Gly Tyr Asp Phe Thr Val Lys Ile Trp Asn Ala His 275 280 285 Thr Gly Arg Cys Ile Arg Thr Leu Thr Gly His Asn Asn Arg Val Tyr 290 295 300 Ser Leu Leu Phe Glu Ser Glu Arg Ser Ile Val Cys Ser Gly Ser Leu 305 310 315 320 Asp Thr Ser Ile Arg Val Trp Asp Phe Thr Arg Pro Glu Gly Gln Glu 325 330 335 Cys Val Ala Leu Leu Gln Gly His Thr Ser Leu Thr Ser Gly Met Gln 340 345 350 Leu Arg Gly Asn Ile Leu Val Ser Cys Asn Ala Asp Ser His Val Arg 355 360 365 Val Trp Asp Ile His Glu Gly Thr Cys Val His Met Leu Ser Gly His 370 375 380 Arg Ser Ala Ile Thr Ser Leu Gln Trp Phe Gly Arg Asn Met Val Ala 385 390 395 400 Thr Ser Ser Asp Asp Gly Thr Val Lys Leu Trp Asp Ile Glu Arg Gly 405 410 415 Ala Leu Ile Arg Asp Leu Val Thr Leu Asp Ser Gly Gly Asn Gly Gly 420 425 430 Cys Ile Trp Arg Leu Cys Ser Thr Ser Thr Met Leu Ala Cys Ala Val 435 440 445 Gly Ser Arg Asn Asn Thr Glu Glu Thr Lys Val Ile Leu Leu Asp Phe 450 455 460 Asp 465 <210> SEQ ID NO 11 <211> LENGTH: 431 <212> TYPE: PRT <213> ORGANISM: Drosophila melanogaster <400> SEQUENCE: 11 Phe Gln Arg Asp Phe Ile Ser Leu Leu Pro Arg Glu Leu Ala Leu Phe 1 5 10 15 Val Leu Ser Tyr Leu Glu Pro Lys Asp Leu Leu Arg Ala Ala Gln Thr 20 25 30 Cys Arg Ser Trp Arg Phe Leu Cys Asp Asp Asn Leu Leu Trp Lys Glu 35 40 45 Lys Cys Arg Lys Ala Gln Ile Leu Ala Glu Pro Arg Ser Asp Arg Pro 50 55 60 Lys Arg Gly Arg Asp Gly Asn Met Pro Pro Ile Ala Ser Pro Trp Lys 65 70 75 80 Ala Ala Tyr Met Arg Gln His Ile Ile Glu Met Asn Trp Arg Ser Arg 85 90 95 Pro Val Arg Lys Pro Lys Val Leu Lys Gly His Asp Asp His Val Ile 100 105 110 Thr Cys Leu Gln Phe Ser Gly Asn Arg Ile Val Ser Gly Ser Asp Asp 115 120 125 Asn Thr Leu Lys Val Trp Ser Ala Val Asn Gly Lys Cys Leu Arg Thr 130 135 140 Leu Val Gly His Thr Gly Gly Val Trp Ser Ser Gln Met Ser Gly Asn 145 150 155 160 Ile Ile Ile Ser Gly Ser Thr Asp Arg Thr Leu Lys Val Trp Asp Met 165 170 175 Asp Ser Gly Ala Cys Val His Thr Leu Gln Gly His Thr Ser Thr Val 180 185 190 Arg Cys Met His Leu His Gly Ser Lys Val Val Ser Gly Ser Arg Asp 195 200 205 Ala Thr Leu Arg Val Trp Asp Ile Glu Gln Gly Ser Cys Leu His Val 210 215 220 Leu Val Gly His Leu Ala Ala Val Arg Cys Val Gln Tyr Asp Gly Lys 225 230 235 240 Leu Ile Val Ser Gly Ala Tyr Asp Tyr Met Val Lys Ile Trp His Pro 245 250 255 Glu Arg Gln Glu Cys Leu His Thr Leu Gln Gly His Thr Asn Arg Val 260 265 270 Tyr Ser Leu Gln Phe Asp Gly Leu His Val Val Ser Gly Ser Leu Asp 275 280 285 Thr Ser Ile Arg Val Trp Asp Val Glu Thr Gly Asn Cys Lys His Thr 290 295 300 Leu Met Gly His Gln Ser Leu Thr Ser Gly Met Glu Leu Arg Gln Asn 305 310 315 320 Ile Leu Val Ser Gly Asn Ala Asp Ser Thr Val Lys Val Trp Asp Ile 325 330 335 Thr Thr Gly Gln Cys Leu Gln Thr Leu Ser Gly Pro Asn Lys His His 340 345 350 Ser Ala Val Thr Cys Leu Gln Phe Asn Ser Arg Phe Val Val Thr Ser 355 360 365 Ser Asp Asp Gly Thr Val Lys Leu Trp Asp Val Lys Thr Gly Asp Phe 370 375 380 Ile Arg Asn Leu Val Ala Leu Asp Ser Gly Gly Ser Gly Gly Val Val 385 390 395 400 Trp Arg Ile Arg Ala Asn Asp Thr Lys Leu Ile Cys Ala Val Gly Ser 405 410 415 Arg Asn Gly Thr Glu Glu Thr Lys Leu Met Val Leu Asp Phe Asp 420 425 430 <210> SEQ ID NO 12 <211> LENGTH: 428 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <400> SEQUENCE: 12 Phe Gln Arg Asp Phe Ile Ser Leu Leu Pro Lys Glu Leu Ala Leu Tyr 1 5 10 15 Val Leu Ser Phe Leu Glu Pro Lys Asp Leu Leu Gln Ala Ala Gln Thr 20 25 30 Cys Arg Tyr Trp Arg Ile Leu Ala Glu Asp Asn Leu Leu Trp Arg Glu 35 40 45 Lys Cys Lys Glu Glu Gly Ile Asp Glu Pro Leu His Ile Lys Arg Arg 50 55 60 Lys Val Ile Lys Pro Gly Phe Ile His Ser Pro Trp Lys Ser Ala Tyr 65 70 75 80 Ile Arg Gln His Arg Ile Asp Thr Asn Trp Arg Arg Gly Glu Leu Lys 85 90 95 Ser Pro Lys Val Leu Lys Gly His Asp Asp His Val Ile Thr Cys Leu 100 105 110 Gln Phe Cys Gly Asn Arg Ile Val Ser Gly Ser Asp Asp Asn Thr Leu 115 120 125 Lys Val Trp Ser Ala Val Thr Gly Lys Cys Leu Arg Thr Leu Val Gly 130 135 140 His Thr Gly Gly Val Trp Ser Ser Gln Met Arg Asp Asn Ile Ile Ile 145 150 155 160 Ser Gly Ser Thr Asp Arg Thr Leu Lys Val Trp Asn Ala Glu Thr Gly 165 170 175 Glu Cys Ile His Thr Leu Tyr Gly His Thr Ser Thr Val Arg Cys Met 180 185 190 His Leu His Glu Lys Arg Val Val Ser Gly Ser Arg Asp Ala Thr Leu 195 200 205 Arg Val Trp Asp Ile Glu Thr Gly Gln Cys Leu His Val Leu Met Gly 210 215 220 His Val Ala Ala Val Arg Cys Val Gln Tyr Asp Gly Arg Arg Val Val 225 230 235 240 Ser Gly Ala Tyr Asp Phe Met Val Lys Val Trp Asp Pro Glu Thr Glu 245 250 255 Thr Cys Leu His Thr Leu Gln Gly His Thr Asn Arg Val Tyr Ser Leu 260 265 270 Gln Phe Asp Gly Ile His Val Val Ser Gly Ser Leu Asp Thr Ser Ile 275 280 285 Arg Val Trp Asp Val Glu Thr Gly Asn Cys Ile His Thr Leu Thr Gly 290 295 300 His Gln Ser Leu Thr Ser Gly Met Glu Leu Lys Asp Asn Ile Leu Val 305 310 315 320 Ser Gly Asn Ala Asp Ser Thr Val Lys Ile Trp Asp Ile Lys Thr Gly 325 330 335 Gln Cys Leu Gln Thr Leu Gln Gly Pro Asn Lys His Gln Ser Ala Val 340 345 350 Thr Cys Leu Gln Phe Asn Lys Asn Phe Val Ile Thr Ser Ser Asp Asp 355 360 365 Gly Thr Val Lys Leu Trp Asp Leu Lys Thr Gly Glu Phe Ile Arg Asn 370 375 380 Leu Val Thr Leu Glu Ser Gly Gly Ser Gly Gly Val Val Trp Arg Ile 385 390 395 400 Arg Ala Ser Asn Thr Lys Leu Val Cys Ala Val Gly Ser Arg Asn Gly 405 410 415 Thr Glu Glu Thr Lys Leu Leu Val Leu Asp Phe Asp 420 425 <210> SEQ ID NO 13 <211> LENGTH: 424 <212> TYPE: PRT <213> ORGANISM: Caenorhabditis elegans <400> SEQUENCE: 13 Leu Gln Arg Asp Phe Ile Ser Asn Leu Pro Ala His Leu Val Glu Leu 1 5 10 15 Ile Leu Phe Asn Val Asn Ser Asp Ser Leu Lys Ser Cys Glu Glu Val 20 25 30 Ser Thr Ser Trp Arg Cys Ala Leu Ala Arg Gly Gln His Trp Lys Lys 35 40 45 Leu Ile Glu Lys Asn Val Arg Ser Asp Ser Leu Trp Trp Gly Leu Ser 50 55 60 Glu Lys Arg Gln Trp Asp Lys Phe Leu Asn Ile Ser Arg Asp Met Ser 65 70 75 80 Val Arg Arg Ile Cys Glu Lys Phe Asn Tyr Asp Val Asn Ile Lys Arg 85 90 95 Asp Lys Leu Asp Gln Leu Ile Leu Met His Val Phe Tyr Ser Lys Leu 100 105 110 Tyr Pro Lys Ile Ile Arg Asp Ile His Asn Ile Asp Asn Asn Trp Lys 115 120 125 Arg Gly Asn Tyr Lys Met Thr Arg Ile Asn Cys Gln Ser Glu Asn Ser 130 135 140 Lys Gly Val Tyr Cys Leu Gln Tyr Asp Asp Asp Lys Ile Val Ser Gly 145 150 155 160 Leu Arg Asp Asn Thr Ile Lys Ile Trp Asp Arg Lys Asp Tyr Ser Cys 165 170 175 Ser Arg Ile Leu Ser Gly His Thr Gly Ser Val Leu Cys Leu Gln Tyr 180 185 190 Asp Asn Arg Val Ile Ile Ser Gly Ser Ser Asp Ala Thr Val Arg Val 195 200 205 Trp Asp Val Glu Thr Gly Glu Cys Ile Lys Thr Leu Ile His His Cys 210 215 220 Glu Ala Val Leu His Leu Arg Phe Ala Asn Gly Ile Met Val Thr Cys 225 230 235 240 Ser Lys Asp Arg Ser Ile Ala Val Trp Asp Met Val Ser Pro Arg Asp 245 250 255 Ile Thr Ile Arg Arg Val Leu Val Gly His Arg Ala Ala Val Asn Val 260 265 270 Val Asp Phe Asp Asp Arg Tyr Ile Val Ser Ala Ser Gly Asp Arg Thr 275 280 285 Ile Lys Val Trp Ser Met Asp Thr Leu Glu Phe Val Arg Thr Leu Ala 290 295 300 Gly His Arg Arg Gly Ile Ala Cys Leu Gln Tyr Arg Gly Arg Leu Val 305 310 315 320 Val Ser Gly Ser Ser Asp Asn Thr Ile Arg Leu Trp Asp Ile His Ser 325 330 335 Gly Val Cys Leu Arg Val Leu Glu Gly His Glu Glu Leu Val Arg Cys 340 345 350 Ile Arg Phe Asp Glu Lys Arg Ile Val Ser Gly Ala Tyr Asp Gly Lys 355 360 365 Ile Lys Val Trp Asp Leu Gln Ala Ala Leu Asp Pro Arg Ala Leu Ser 370 375 380 Ser Glu Ile Cys Leu Cys Ser Leu Val Gln His Thr Gly Arg Val Phe 385 390 395 400 Arg Leu Gln Phe Asp Asp Phe Gln Ile Val Ser Ser Ser His Asp Asp 405 410 415 Thr Ile Leu Ile Trp Asp Phe Leu 420 <210> SEQ ID NO 14 <211> LENGTH: 407 <212> TYPE: PRT <213> ORGANISM: Drosophila melanogaster <400> SEQUENCE: 14 Leu Gln Arg Asp Phe Ile Thr Leu Leu Pro Ile Lys Gly Leu Asp His 1 5 10 15 Ile Ala Glu Asn Ile Leu Ser Tyr Leu Asp Ala Glu Ser Leu Lys Ser 20 25 30 Ser Glu Leu Val Cys Lys Glu Trp Leu Arg Val Ile Ser Glu Gly Met 35 40 45 Leu Trp Lys Lys Leu Ile Glu Arg Lys Val Arg Thr Asp Ser Leu Trp 50 55 60 Arg Gly Leu Ala Glu Arg Arg Asn Trp Met Gln Tyr Leu Phe Lys Pro 65 70 75 80 Arg Pro Gly Gln Thr Gln Arg Pro His Ser Phe His Arg Glu Leu Phe 85 90 95 Pro Lys Ile Met Asn Asp Ile Asp Ser Ile Glu Asn Asn Trp Arg Thr 100 105 110 Gly Arg His Met Leu Arg Arg Ile Asn Cys Arg Ser Glu Asn Ser Lys 115 120 125 Gly Val Tyr Cys Leu Gln Tyr Asp Asp Gly Lys Ile Val Ser Gly Leu 130 135 140 Arg Asp Asn Thr Ile Lys Ile Trp Asp Arg Thr Asp Leu Gln Cys Val 145 150 155 160 Lys Thr Leu Met Gly His Thr Gly Ser Val Leu Cys Leu Gln Tyr Asp 165 170 175 Asp Lys Val Ile Ile Ser Gly Ser Ser Asp Ser Thr Val Arg Val Trp 180 185 190 Asp Val Asn Thr Gly Glu Met Val Asn Thr Leu Ile His His Cys Glu 195 200 205 Ala Val Leu His Leu Arg Phe Asn Asn Gly Met Met Val Thr Cys Ser 210 215 220 Lys Asp Arg Ser Ile Ala Val Trp Asp Met Thr Ser Pro Ser Glu Ile 225 230 235 240 Thr Leu Arg Arg Val Leu Val Gly His Arg Ala Ala Val Asn Val Val 245 250 255 Asp Phe Asp Glu Lys Tyr Ile Val Ser Ala Ser Gly Asp Arg Thr Ile 260 265 270 Lys Val Trp Ser Thr Ser Ser Cys Glu Phe Val Arg Thr Leu Asn Gly 275 280 285 His Lys Arg Gly Ile Ala Cys Leu Gln Tyr Arg Asp Arg Leu Val Val 290 295 300 Ser Gly Ser Ser Asp Asn Ser Ile Arg Leu Trp Asp Ile Glu Cys Gly 305 310 315 320 Ala Cys Leu Arg Val Leu Glu Gly His Glu Glu Leu Val Arg Cys Ile 325 330 335 Arg Phe Asp Thr Lys Arg Ile Val Ser Gly Ala Tyr Asp Gly Lys Ile 340 345 350 Lys Val Trp Asp Leu Val Ala Ala Leu Asp Pro Arg Ala Ala Ser Asn 355 360 365 Thr Leu Cys Leu Asn Thr Leu Val Glu His Thr Gly Arg Val Phe Arg 370 375 380 Leu Gln Phe Asp Glu Phe Gln Ile Val Ser Ser Ser His Asp Asp Thr 385 390 395 400 Ile Leu Ile Trp Asp Phe Leu 405 <210> SEQ ID NO 15 <211> LENGTH: 408 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <400> SEQUENCE: 15 Leu Gln Arg Asp Phe Ile Thr Ala Leu Pro Ala Arg Gly Leu Asp His 1 5 10 15 Ile Ala Glu Asn Ile Leu Ser Tyr Leu Asp Ala Lys Ser Leu Cys Ala 20 25 30 Ala Glu Leu Val Cys Lys Glu Trp Tyr Arg Val Thr Ser Asp Gly Met 35 40 45 Leu Trp Lys Lys Leu Ile Glu Arg Met Val Arg Thr Asp Ser Leu Trp 50 55 60 Arg Gly Leu Ala Glu Arg Arg Gly Trp Gly Gln Tyr Leu Phe Lys Asn 65 70 75 80 Lys Pro Pro Asp Gly Asn Ala Pro Pro Asn Ser Phe Tyr Arg Ala Leu 85 90 95 Tyr Pro Lys Ile Ile Gln Asp Ile Glu Thr Ile Glu Ser Asn Trp Arg 100 105 110 Cys Gly Arg His Ser Leu Gln Arg Ile His Cys Arg Ser Glu Thr Ser 115 120 125 Lys Gly Val Tyr Cys Leu Gln Tyr Asp Asp Gln Lys Ile Val Ser Gly 130 135 140 Leu Arg Asp Asn Thr Ile Lys Ile Trp Asp Lys Asn Thr Leu Glu Cys 145 150 155 160 Lys Arg Ile Leu Thr Gly His Thr Gly Ser Val Leu Cys Leu Gln Tyr 165 170 175 Asp Glu Arg Val Ile Ile Thr Gly Ser Ser Asp Ser Thr Val Arg Val 180 185 190 Trp Asp Val Asn Thr Gly Glu Met Leu Asn Thr Leu Ile His His Cys 195 200 205 Glu Ala Val Leu His Leu Arg Phe Asn Asn Gly Met Met Val Thr Cys 210 215 220 Ser Lys Asp Arg Ser Ile Ala Val Trp Asp Met Ala Ser Pro Thr Asp 225 230 235 240 Ile Thr Leu Arg Arg Val Leu Val Gly His Arg Ala Ala Val Asn Val 245 250 255 Val Asp Phe Asp Asp Lys Tyr Ile Val Ser Ala Ser Gly Asp Arg Thr 260 265 270 Ile Lys Val Trp Asn Thr Ser Thr Cys Glu Phe Val Arg Thr Leu Asn 275 280 285 Gly His Lys Arg Gly Ile Ala Cys Leu Gln Tyr Arg Asp Arg Leu Val 290 295 300 Val Ser Gly Ser Ser Asp Asn Thr Ile Arg Leu Trp Asp Ile Glu Cys 305 310 315 320 Gly Ala Cys Leu Arg Val Leu Glu Gly His Glu Glu Leu Val Arg Cys 325 330 335 Ile Arg Phe Asp Asn Lys Arg Ile Val Ser Gly Ala Tyr Asp Gly Lys 340 345 350 Ile Lys Val Trp Asp Leu Val Ala Ala Leu Asp Pro Arg Ala Pro Ala 355 360 365 Gly Thr Leu Cys Leu Arg Thr Leu Val Glu His Ser Gly Arg Val Phe 370 375 380 Arg Leu Gln Phe Asp Glu Phe Gln Ile Val Ser Ser Ser His Asp Asp 385 390 395 400 Thr Ile Leu Ile Trp Asp Phe Leu 405 <210> SEQ ID NO 16 <211> LENGTH: 459 <212> TYPE: PRT <213> ORGANISM: Saccharomyces cerevisiae <400> SEQUENCE: 16 Ile Lys Ile Asp Phe Ile Ser Ile Leu Pro Gln Glu Leu Ser Leu Lys 1 5 10 15 Ile Leu Ser Tyr Leu Asp Cys Gln Ser Leu Cys Asn Ala Thr Arg Val 20 25 30 Cys Arg Lys Trp Gln Lys Leu Ala Asp Asp Asp Arg Val Trp Tyr His 35 40 45 Met Cys Glu Gln His Ile Asp Arg Lys Cys Pro Asn Cys Gly Trp Gly 50 55 60 Leu Pro Leu Leu His Met Lys Arg Ala Arg Ile Gln Gln Asn Ser Thr 65 70 75 80 Gly Ser Ser Ser Asn Ala Asp Ile Gln Thr Gln Thr Thr Arg Pro Trp 85 90 95 Lys Val Ile Tyr Arg Glu Arg Phe Lys Val Glu Ser Asn Trp Arg Lys 100 105 110 Gly His Cys Arg Ile Gln Glu Phe Lys Gly His Met Asp Gly Val Leu 115 120 125 Thr Leu Gln Phe Asn Tyr Arg Leu Leu Phe Thr Gly Ser Tyr Asp Ser 130 135 140 Thr Ile Gly Ile Trp Asp Leu Phe Thr Gly Lys Leu Ile Arg Arg Leu 145 150 155 160 Ser Gly His Ser Asp Gly Val Lys Thr Leu Tyr Phe Asp Asp Arg Lys 165 170 175 Leu Ile Thr Gly Ser Leu Asp Lys Thr Ile Arg Val Trp Asn Tyr Ile 180 185 190 Thr Gly Glu Cys Ile Ser Thr Tyr Arg Gly His Ser Asp Ser Val Leu 195 200 205 Ser Val Asp Ser Tyr Gln Lys Val Ile Val Ser Gly Ser Ala Asp Lys 210 215 220 Thr Val Lys Val Trp His Val Glu Ser Arg Thr Cys Tyr Thr Leu Arg 225 230 235 240 Gly His Thr Glu Trp Val Asn Cys Val Lys Leu His Pro Lys Ser Phe 245 250 255 Ser Cys Phe Ser Cys Ser Asp Asp Thr Thr Ile Arg Met Trp Asp Ile 260 265 270 Arg Thr Asn Ser Cys Leu Lys Val Phe Arg Gly His Val Gly Gln Val 275 280 285 Gln Lys Ile Ile Pro Leu Thr Ile Lys Asp Val Glu Asn Leu Ala Thr 290 295 300 Asp Asn Thr Ser Asp Gly Ser Ser Pro Gln Asp Asp Pro Thr Met Thr 305 310 315 320 Asp Gly Ala Asp Glu Ser Asp Thr Pro Ser Asn Glu Gln Glu Thr Val 325 330 335 Leu Asp Glu Asn Ile Pro Tyr Pro Thr His Leu Leu Ser Cys Gly Leu 340 345 350 Asp Asn Thr Ile Lys Leu Trp Asp Val Lys Thr Gly Lys Cys Ile Arg 355 360 365 Thr Gln Phe Gly His Val Glu Gly Val Trp Asp Ile Ala Ala Asp Asn 370 375 380 Phe Arg Ile Ile Ser Gly Ser His Asp Gly Ser Ile Lys Val Trp Asp 385 390 395 400 Leu Gln Ser Gly Lys Cys Met His Thr Phe Asn Gly Arg Arg Leu Gln 405 410 415 Arg Glu Thr Gln His Thr Gln Thr Gln Ser Leu Gly Asp Lys Val Ala 420 425 430 Pro Ile Ala Cys Val Cys Ile Gly Asp Ser Glu Cys Phe Ser Gly Asp 435 440 445 Glu Phe Gly Cys Val Lys Met Tyr Lys Phe Asp 450 455 <210> SEQ ID NO 17 <211> LENGTH: 640 <212> TYPE: PRT <213> ORGANISM: Saccharomyces cerevisiae <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/P39014 <309> DATABASE ENTRY DATE: 1995-02-01 <313> RELEVANT RESIDUES: (1)..(640) <400> SEQUENCE: 17 Met Arg Arg Glu Arg Gln Arg Met Met Ser Phe Glu Asp Lys Asp Lys 1 5 10 15 Asp Asp Leu Asp Asn Ser Asn Ser Asn Asn Ser Ser Glu Met Thr Asp 20 25 30 Thr Ala Met Met Pro Pro Leu Lys Arg Leu Leu Ile Thr Gly Ser Ser 35 40 45 Asp Asp Leu Ala Gln Gly Ser Ser Gly Lys Lys Lys Met Thr Met Ala 50 55 60 Thr Arg Ser Pro Ser Ser Ser Pro Asp Leu Ala Thr Asn Asp Ser Gly 65 70 75 80 Thr Arg Val Gln Pro Leu Pro Glu Tyr Asn Phe Thr Lys Phe Cys Tyr 85 90 95 Arg His Asn Pro Asp Ile Gln Phe Ser Pro Thr His Thr Ala Cys Tyr 100 105 110 Lys Gln Asp Leu Lys Arg Thr Gln Glu Ile Asn Ala Asn Ile Ala Lys 115 120 125 Leu Pro Leu Gln Glu Gln Ser Asp Ile His His Ile Ile Ser Lys Tyr 130 135 140 Ser Asn Ser Asn Asp Lys Ile Arg Lys Leu Ile Leu Asp Gly Ile Leu 145 150 155 160 Ser Thr Ser Cys Phe Pro Gln Leu Ser Tyr Ile Ser Ser Leu Val Thr 165 170 175 His Met Ile Lys Ile Asp Phe Ile Ser Ile Leu Pro Gln Glu Leu Ser 180 185 190 Leu Lys Ile Leu Ser Tyr Leu Asp Cys Gln Ser Leu Cys Asn Ala Thr 195 200 205 Arg Val Cys Arg Lys Trp Gln Lys Leu Ala Asp Asp Asp Arg Val Trp 210 215 220 Tyr His Met Cys Glu Gln His Ile Asp Arg Lys Cys Pro Asn Cys Gly 225 230 235 240 Trp Gly Leu Pro Leu Leu His Met Lys Arg Ala Arg Ile Gln Gln Asn 245 250 255 Ser Thr Gly Ser Ser Ser Asn Ala Asp Ile Gln Thr Gln Thr Thr Arg 260 265 270 Pro Trp Lys Val Ile Tyr Arg Glu Arg Phe Lys Val Glu Ser Asn Trp 275 280 285 Arg Lys Gly His Cys Arg Ile Gln Glu Phe Lys Gly His Met Asp Gly 290 295 300 Val Leu Thr Leu Gln Phe Asn Tyr Arg Leu Leu Phe Thr Gly Ser Tyr 305 310 315 320 Asp Ser Thr Ile Gly Ile Trp Asp Leu Phe Thr Gly Lys Leu Ile Arg 325 330 335 Arg Leu Ser Gly His Ser Asp Gly Val Lys Thr Leu Tyr Phe Asp Asp 340 345 350 Arg Lys Leu Ile Thr Gly Ser Leu Asp Lys Thr Ile Arg Val Trp Asn 355 360 365 Tyr Ile Thr Gly Glu Cys Ile Ser Thr Tyr Arg Gly His Ser Asp Ser 370 375 380 Val Leu Ser Val Asp Ser Tyr Gln Lys Val Ile Val Ser Gly Ser Ala 385 390 395 400 Asp Lys Thr Val Lys Val Trp His Val Glu Ser Arg Thr Cys Tyr Thr 405 410 415 Leu Arg Gly His Thr Glu Trp Val Asn Cys Val Lys Leu His Pro Lys 420 425 430 Ser Phe Ser Cys Phe Ser Cys Ser Asp Asp Thr Thr Ile Arg Met Trp 435 440 445 Asp Ile Arg Thr Asn Ser Cys Leu Lys Val Phe Arg Gly His Val Gly 450 455 460 Gln Val Gln Lys Ile Ile Pro Leu Thr Ile Lys Asp Val Glu Asn Leu 465 470 475 480 Ala Thr Asp Asn Thr Ser Asp Gly Ser Ser Pro Gln Asp Asp Pro Thr 485 490 495 Met Thr Asp Gly Ala Asp Glu Ser Asp Thr Pro Ser Asn Glu Gln Glu 500 505 510 Thr Val Leu Asp Glu Asn Ile Pro Tyr Pro Thr His Leu Leu Ser Cys 515 520 525 Gly Leu Asp Asn Thr Ile Lys Leu Trp Asp Val Lys Thr Gly Lys Cys 530 535 540 Ile Arg Thr Gln Phe Gly His Val Glu Gly Val Trp Asp Ile Ala Ala 545 550 555 560 Asp Asn Phe Arg Ile Ile Ser Gly Ser His Asp Gly Ser Ile Lys Val 565 570 575 Trp Asp Leu Gln Ser Gly Lys Cys Met His Thr Phe Asn Gly Arg Arg 580 585 590 Leu Gln Arg Glu Thr Gln His Thr Gln Thr Gln Ser Leu Gly Asp Lys 595 600 605 Val Ala Pro Ile Ala Cys Val Cys Ile Gly Asp Ser Glu Cys Phe Ser 610 615 620 Gly Asp Glu Phe Gly Cys Val Lys Met Tyr Lys Phe Asp Leu Asn Asp 625 630 635 640 <210> SEQ ID NO 18 <211> LENGTH: 569 <212> TYPE: PRT <213> ORGANISM: Mus musculus <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/NP_033901 <309> DATABASE ENTRY DATE: 1998-08-04 <313> RELEVANT RESIDUES: (1)..(569) <400> SEQUENCE: 18 Met Asp Pro Ala Glu Ala Val Leu Gln Glu Lys Ala Leu Lys Phe Met 1 5 10 15 Asn Ser Ser Glu Arg Glu Asp Cys Asn Asn Gly Glu Pro Pro Arg Lys 20 25 30 Ile Ile Pro Glu Lys Asn Ser Leu Arg Gln Thr Tyr Asn Ser Cys Ala 35 40 45 Arg Leu Cys Ile Asn Gln Glu Thr Val Cys Leu Thr Ser Thr Ala Met 50 55 60 Lys Thr Glu Asn Cys Val Ala Lys Ala Lys Leu Ala Asn Gly Thr Ser 65 70 75 80 Ser Met Ile Val Pro Lys Gln Arg Lys Leu Ser Ala Ser Tyr Glu Lys 85 90 95 Glu Lys Glu Leu Cys Val Lys Tyr Phe Glu Gln Trp Ser Glu Ser Asp 100 105 110 Gln Val Glu Phe Val Glu His Leu Ile Ser Gln Met Cys His Tyr Gln 115 120 125 His Gly His Ile Asn Ser Tyr Leu Lys Pro Met Leu Gln Arg Asp Phe 130 135 140 Ile Thr Ala Leu Pro Ala Arg Gly Leu Asp His Ile Ala Glu Asn Ile 145 150 155 160 Leu Ser Tyr Leu Asp Ala Lys Ser Leu Cys Ala Ala Glu Leu Val Cys 165 170 175 Lys Glu Trp Tyr Arg Val Thr Ser Asp Gly Met Leu Trp Lys Lys Leu 180 185 190 Ile Glu Arg Met Val Arg Thr Asp Ser Leu Trp Arg Gly Leu Ala Glu 195 200 205 Arg Arg Gly Trp Gly Gln Tyr Leu Phe Lys Asn Lys Pro Pro Asp Glu 210 215 220 Asn Ala Pro Pro Asn Ser Phe Tyr Arg Ala Leu Tyr Pro Lys Ile Ile 225 230 235 240 Gln Asp Ile Glu Thr Ile Glu Ser Asn Trp Arg Cys Gly Arg His Ser 245 250 255 Leu Gln Arg Ile His Cys Arg Ser Glu Thr Ser Lys Gly Val Tyr Cys 260 265 270 Leu Gln Tyr Asp Asp Gln Lys Ile Val Ser Gly Leu Arg Asp Asn Thr 275 280 285 Ile Lys Ile Trp Asp Lys Ser Thr Leu Glu Cys Lys Arg Ile Leu Thr 290 295 300 Gly His Thr Gly Ser Val Leu Cys Leu Gln Tyr Asp Glu Arg Val Ile 305 310 315 320 Ile Thr Gly Ser Ser Asp Ser Thr Val Arg Val Trp Asp Val Asn Ala 325 330 335 Gly Glu Met Leu Asn Thr Leu Ile His His Cys Glu Ala Val Leu His 340 345 350 Leu Arg Phe Asn Asn Gly Met Met Val Thr Cys Ser Lys Asp Arg Ser 355 360 365 Ile Ala Val Trp Asp Met Ala Ser Pro Thr Asp Ile Thr Leu Arg Arg 370 375 380 Val Leu Val Gly His Arg Ala Ala Val Asn Val Val Asp Phe Asp Asp 385 390 395 400 Lys Tyr Ile Val Ser Ala Ser Gly Asp Arg Thr Ile Lys Val Trp Asn 405 410 415 Thr Ser Thr Cys Glu Phe Val Arg Thr Leu Asn Gly His Lys Arg Gly 420 425 430 Ile Ala Cys Leu Gln Tyr Arg Asp Arg Leu Val Val Ser Gly Ser Ser 435 440 445 Asp Asn Thr Ile Arg Leu Trp Asp Ile Glu Cys Gly Ala Cys Leu Arg 450 455 460 Val Leu Glu Gly His Glu Glu Leu Val Arg Cys Ile Arg Phe Asp Asn 465 470 475 480 Lys Arg Ile Val Ser Gly Ala Tyr Asp Gly Lys Ile Lys Val Trp Asp 485 490 495 Leu Met Ala Ala Leu Asp Pro Arg Ala Pro Ala Gly Thr Leu Cys Leu 500 505 510 Arg Thr Leu Val Glu His Ser Gly Arg Val Phe Arg Leu Gln Phe Asp 515 520 525 Glu Phe Gln Ile Val Ser Ser Ser His Asp Asp Thr Ile Leu Ile Trp 530 535 540 Asp Phe Leu Asn Asp Pro Ala Ala His Ala Glu Pro Pro Arg Ser Pro 545 550 555 560 Ser Arg Thr Tyr Thr Tyr Ile Ser Arg 565 <210> SEQ ID NO 19 <211> LENGTH: 5 <212> TYPE: PRT <213> ORGANISM: Peptide Motif <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (1)..(1) <223> OTHER INFORMATION: wherein Xaa can be Leu, Pro, or Ile <220> FEATURE: <221> NAME/KEY: DOMAIN <222> LOCATION: (1)..(5) <223> OTHER INFORMATION: Cdc4 Phospho-Degron motif <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (2)..(2) <223> OTHER INFORMATION: wherein Xaa can be any naturally occurring amino acid <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (5)..(5) <223> OTHER INFORMATION: wherein Xaa can be any naturally occurring amino acid except basic and bulky hydrophobic amino acids <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (5)..(5) <223> OTHER INFORMATION: wherein Xaa can be any naturally occurring amino acid <400> SEQUENCE: 19 Xaa Xaa Pro Thr Xaa 1 5 <210> SEQ ID NO 20 <211> LENGTH: 8 <212> TYPE: PRT <213> ORGANISM: Peptide Motif <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (1)..(1) <223> OTHER INFORMATION: wherein Xaa can be Leu, Pro, or Ile <220> FEATURE: <221> NAME/KEY: DOMAIN <222> LOCATION: (1)..(8) <223> OTHER INFORMATION: Cdc4 Phospho-Degron motif <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (2)..(2) <223> OTHER INFORMATION: wherein Xaa can be Leu, Ile, Val, or Pro <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (5)..(5) <223> OTHER INFORMATION: wherein Xaa can be any naturally occurring amino acid except basic and bulky hydrophobic amino acids <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (6)..(6) <223> OTHER INFORMATION: wherein Xaa can be any naturally occurring amino acid <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (7)..(7) <223> OTHER INFORMATION: wherein Xaa can be any naturally occurring amino acid <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (8)..(8) <223> OTHER INFORMATION: wherein Xaa can be any naturally occurring amino acid <400> SEQUENCE: 20 Xaa Xaa Thr Pro Xaa Xaa Xaa Xaa 1 5 <210> SEQ ID NO 21 <211> LENGTH: 4 <212> TYPE: PRT <213> ORGANISM: Peptide Motif <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (1)..(1) <223> OTHER INFORMATION: wherein Xaa can be Leu, Gly or Thr <220> FEATURE: <221> NAME/KEY: DOMAIN <222> LOCATION: (1)..(4) <223> OTHER INFORMATION: Cdc4 Phospho-Degron motif <400> SEQUENCE: 21 Xaa Pro Thr Pro 1 <210> SEQ ID NO 22 <211> LENGTH: 779 <212> TYPE: PRT <213> ORGANISM: Saccharomyces cerevisiae <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/S56245 <309> DATABASE ENTRY DATE: 1993-05-07 <313> RELEVANT RESIDUES: (1)..(51) <400> SEQUENCE: 22 Met Gly Ser Phe Pro Leu Ala Glu Phe Pro Leu Arg Asp Ile Pro Val 1 5 10 15 Pro Tyr Ser Tyr Arg Val Ser Gly Gly Ile Ala Ser Ser Gly Ser Val 20 25 30 Thr Ala Leu Val Thr Ala Ala Gly Thr His Arg Asn Ser Ser Thr Ala 35 40 45 Lys Thr Val Glu Thr Glu Asp Gly Glu Glu Asp Ile Asp Glu Tyr Gln 50 55 60 Arg Lys Arg Ala Ala Gly Ser Gly Glu Ser Thr Pro Glu Arg Ser Asp 65 70 75 80 Phe Lys Arg Val Lys His Asp Asn His Lys Thr Leu His Pro Val Asn 85 90 95 Leu Gln Asn Thr Gly Ala Ala Ser Val Asp Asn Asp Gly Leu His Asn 100 105 110 Leu Thr Asp Ile Ser Asn Asp Ala Glu Lys Leu Leu Met Ser Val Asp 115 120 125 Asp Gly Ser Ala Ala Pro Ser Thr Leu Ser Val Asn Met Gly Val Ala 130 135 140 Ser His Asn Val Ala Ala Pro Thr Thr Val Asn Ala Ala Thr Ile Thr 145 150 155 160 Gly Ser Asp Val Ser Asn Asn Val Asn Ser Ala Thr Ile Asn Asn Pro 165 170 175 Met Glu Glu Gly Ala Leu Pro Leu Ser Pro Thr Ala Ser Ser Pro Gly 180 185 190 Thr Thr Thr Pro Leu Ala Lys Thr Thr Lys Thr Ile Asn Asn Asn Asn 195 200 205 Asn Ile Ala Asp Leu Ile Glu Ser Lys Asp Ser Ile Ile Ser Pro Glu 210 215 220 Tyr Leu Ser Asp Glu Ile Phe Ser Ala Ile Asn Asn Asn Leu Pro His 225 230 235 240 Ala Tyr Phe Lys Asn Leu Leu Phe Arg Leu Val Ala Asn Met Asp Arg 245 250 255 Ser Glu Leu Ser Asp Leu Gly Thr Leu Ile Lys Asp Asn Leu Lys Arg 260 265 270 Asp Leu Ile Thr Ser Leu Pro Phe Glu Ile Ser Leu Lys Ile Phe Asn 275 280 285 Tyr Leu Gln Phe Glu Asp Ile Ile Asn Ser Leu Gly Val Ser Gln Asn 290 295 300 Trp Asn Lys Ile Ile Arg Lys Ser Thr Ser Leu Trp Lys Lys Leu Leu 305 310 315 320 Ile Ser Glu Asn Phe Val Ser Pro Lys Gly Phe Asn Ser Leu Asn Leu 325 330 335 Lys Leu Ser Gln Lys Tyr Pro Lys Leu Ser Gln Gln Asp Arg Leu Arg 340 345 350 Leu Ser Phe Leu Glu Asn Ile Phe Ile Leu Lys Asn Trp Tyr Asn Pro 355 360 365 Lys Phe Val Pro Gln Arg Thr Thr Leu Arg Gly His Met Thr Ser Val 370 375 380 Ile Thr Cys Leu Gln Phe Glu Asp Asn Tyr Val Ile Thr Gly Ala Asp 385 390 395 400 Asp Lys Met Ile Arg Val Tyr Asp Ser Ile Asn Lys Lys Phe Leu Leu 405 410 415 Gln Leu Ser Gly His Asp Gly Gly Val Trp Ala Leu Lys Tyr Ala His 420 425 430 Gly Gly Ile Leu Val Ser Gly Ser Thr Asp Arg Thr Val Arg Val Trp 435 440 445 Asp Ile Lys Lys Gly Cys Cys Thr His Val Phe Lys Gly His Asn Ser 450 455 460 Thr Val Arg Cys Leu Asp Ile Val Glu Tyr Lys Asn Ile Lys Tyr Ile 465 470 475 480 Val Thr Gly Ser Arg Asp Asn Thr Leu His Val Trp Lys Leu Pro Lys 485 490 495 Glu Ser Ser Val Pro Asp His Gly Glu Glu His Asp Tyr Pro Leu Val 500 505 510 Phe His Thr Pro Glu Glu Asn Pro Tyr Phe Val Gly Val Leu Arg Gly 515 520 525 His Met Ala Ser Val Arg Thr Val Ser Gly His Gly Asn Ile Val Val 530 535 540 Ser Gly Ser Tyr Asp Asn Thr Leu Ile Val Trp Asp Val Ala Gln Met 545 550 555 560 Lys Cys Leu Tyr Ile Leu Ser Gly His Thr Asp Arg Ile Tyr Ser Thr 565 570 575 Ile Tyr Asp His Glu Arg Lys Arg Cys Ile Ser Ala Ser Met Asp Thr 580 585 590 Thr Ile Arg Ile Trp Asp Leu Glu Asn Ile Trp Asn Asn Gly Glu Cys 595 600 605 Ser Tyr Ala Thr Asn Ser Ala Ser Pro Cys Ala Lys Ile Leu Gly Ala 610 615 620 Met Tyr Thr Leu Gln Gly His Thr Ala Leu Val Gly Leu Leu Arg Leu 625 630 635 640 Ser Asp Lys Phe Leu Val Ser Ala Ala Ala Asp Gly Ser Ile Arg Gly 645 650 655 Trp Asp Ala Asn Asp Tyr Ser Arg Lys Phe Ser Tyr His His Thr Asn 660 665 670 Leu Ser Ala Ile Thr Thr Phe Tyr Val Ser Asp Asn Ile Leu Val Ser 675 680 685 Gly Ser Glu Asn Gln Phe Asn Ile Tyr Asn Leu Arg Ser Gly Lys Leu 690 695 700 Val His Ala Asn Ile Leu Lys Asp Ala Asp Gln Ile Trp Ser Val Asn 705 710 715 720 Phe Lys Gly Lys Thr Leu Val Ala Ala Val Glu Lys Asp Gly Gln Ser 725 730 735 Phe Leu Glu Ile Leu Asp Phe Ser Lys Ala Ser Lys Ile Asn Tyr Val 740 745 750 Ser Asn Pro Val Asn Ser Ser Ser Ser Ser Leu Glu Ser Ile Ser Thr 755 760 765 Ser Leu Gly Leu Thr Arg Thr Thr Ile Ile Pro 770 775 <210> SEQ ID NO 23 <211> LENGTH: 684 <212> TYPE: PRT <213> ORGANISM: Candida albicans <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/CAA65538 <309> DATABASE ENTRY DATE: 1996-04-04 <313> RELEVANT RESIDUES: (1)..(684) <400> SEQUENCE: 23 Met Pro Ser Cys Asp Asp Thr Ala Ser Ser Asp Thr Asp Cys Gln Ser 1 5 10 15 Gln Val Ser Ser Thr Ala His Leu His Ser Tyr Arg Ser Asn Gly Leu 20 25 30 Val Glu Pro Pro Ser Lys Arg Arg Leu Thr Thr Thr Asn Glu Thr Ser 35 40 45 Leu Ser Ser Ala Gly Ala Thr Thr Phe Gln Ile Glu Ser Pro Gly Ser 50 55 60 Ile Ser Ala Ile Thr Thr Asn Asn Ser Thr Thr Ser Ala Gly Asp Ser 65 70 75 80 Asn Asn Ser Asn Ser Phe Ser Asp Gln His Ser Arg His Pro Arg Thr 85 90 95 Pro Asn Ala Met Asn Ser Pro Thr His Thr Pro Ile Ser Asp Ile Glu 100 105 110 Glu Asp Pro Ile Gln Gln Leu Pro Leu Pro Ser Pro Ser Ala Ser Pro 115 120 125 Ile Gln Ser Asp Thr Glu Asn Glu His Val Thr Thr Pro Asp Ser Leu 130 135 140 Gln Gly Lys Ala Asn Leu Asp Ser Ile Glu Asn Val Met Ser Asn Glu 145 150 155 160 Pro Thr Thr Gln Ser Glu Leu Val Asp Leu Val Thr Lys Leu Ser Gly 165 170 175 Phe Leu Ser Glu Ala Asn Gln Asn His Leu Val Phe Lys Leu Leu Gln 180 185 190 Lys Thr Thr Arg Pro Thr Leu Ser Thr Phe Asn Asn Leu Ile Asn Asn 195 200 205 Ser Leu Lys Arg Asp Ile Leu Ser Asn Val Pro Phe Glu Val Thr Met 210 215 220 Lys Ile Leu Ser Tyr Leu Asp Tyr Lys Thr Leu Leu Ser Val Ala Gln 225 230 235 240 Val Cys Lys Lys Trp Phe Asp Ile Ile Asn Asn Pro Asp Thr Trp Ile 245 250 255 Lys Leu Leu Lys Arg Asp Lys Leu Ile Thr Asp Asp Ala Val Ile Lys 260 265 270 Tyr Glu Leu Gln Tyr Pro Asp Gln Leu Leu Arg Glu Trp Ser Thr Leu 275 280 285 Pro Glu Ile Asn Ser Ala Gln Val Leu Tyr Lys Lys Arg Lys Ile Ile 290 295 300 Val Asn Arg Trp Met Asp Pro Lys Phe Lys Pro His Arg Ile Ser Val 305 310 315 320 Ser Gly His Gly Asn Lys Val Val Thr Cys Leu Gln His Asp Asp Glu 325 330 335 Lys Val Val Thr Gly Val Asp Asp Lys Cys Ile Ser Ile Tyr Ser Thr 340 345 350 Gln Thr Gly Gln Leu Met Lys Val Leu Glu Gly His Glu Gly Gly Val 355 360 365 Trp Ala Leu Lys Tyr Thr Gly Asn Thr Leu Val Thr Gly Ser Thr Asp 370 375 380 Arg Thr Val Arg Val Trp Asn Met Lys Thr Gly Gln Cys Thr His Ile 385 390 395 400 Phe Arg Gly His Thr Ser Thr Ile Arg Cys Leu Asp Ile Ile His Pro 405 410 415 Ala Val Ile Gly Lys Asn Gln Asp Gly Glu Asp Ile Val Phe Pro Glu 420 425 430 Tyr Pro Leu Leu Ile Thr Gly Ser Arg Asp His Asn Ile His Val Trp 435 440 445 Lys Leu Pro Val Val Asp Asp Ser Gln Asp Tyr Ile Glu Thr Phe Glu 450 455 460 Gly Glu Phe Asp Asn Pro Tyr Leu Ile Ala Val Leu Ser Gly His Thr 465 470 475 480 Gln Ser Val Arg Ser Ile Ser Gly Tyr Gly Asn Ile Ile Ile Ser Gly 485 490 495 Ser Tyr Asp Ser Thr Val Arg Val Trp Asp Leu Leu Asp Asp Gly His 500 505 510 Cys Thr His Val Leu Gln Gly His Leu Asp Arg Val Tyr Ser Thr Ala 515 520 525 Ile Asp Phe His Ser Lys Thr Cys Phe Ser Gly Ser Met Asp Ser Asn 530 535 540 Ile Asn Val Trp Asn Phe Glu Thr Gly Glu Leu Lys Lys Val Leu Val 545 550 555 560 Gly His Ala Ser Leu Val Gly Leu Leu Asp Leu Val Asp Asp Val Leu 565 570 575 Val Ser Ala Ala Ala Asp Ala Thr Leu Arg Ile Trp Asp Ala Lys Thr 580 585 590 Gly Glu Leu Arg Ser Lys Leu Lys Gly His Gly Ala Ala Ile Thr Cys 595 600 605 Phe Glu His Asp Gly Leu Arg Val Val Ser Gly Ser Glu Lys Met Leu 610 615 620 Lys Leu Trp Asn Val Glu Lys Gly Thr Phe Ala Arg Asp Leu Leu Ser 625 630 635 640 Asp Val Thr Gly Gly Ile Trp Gln Val Arg Phe Asp Tyr Lys Arg Cys 645 650 655 Val Ala Ala Val Gln Arg Ile Ile Asn Glu Asp Glu Gly Glu Thr Phe 660 665 670 Ile Glu Ile Leu Asp Phe Ser Gln Pro Leu Leu Gln 675 680 <210> SEQ ID NO 24 <211> LENGTH: 707 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/AAL07271 <309> DATABASE ENTRY DATE: 2001-08-30 <313> RELEVANT RESIDUES: (1)..(707) <400> SEQUENCE: 24 Met Asn Gln Glu Leu Leu Ser Val Gly Ser Lys Arg Arg Arg Thr Gly 1 5 10 15 Gly Ser Leu Arg Gly Asn Pro Ser Ser Ser Gln Val Asp Glu Glu Gln 20 25 30 Met Asn Arg Val Val Glu Glu Glu Gln Gln Gln Gln Leu Arg Gln Gln 35 40 45 Glu Glu Glu His Thr Ala Arg Asn Gly Glu Val Val Gly Val Glu Pro 50 55 60 Arg Pro Gly Gly Gln Asn Asp Ser Gln Gln Gly Gln Leu Glu Glu Asn 65 70 75 80 Asn Asn Arg Phe Ile Ser Val Asp Glu Asp Ser Ser Gly Asn Gln Glu 85 90 95 Glu Gln Glu Glu Asp Glu Glu His Ala Gly Glu Gln Asp Glu Glu Asp 100 105 110 Glu Glu Glu Glu Glu Met Asp Gln Glu Ser Asp Asp Phe Asp Gln Ser 115 120 125 Asp Asp Ser Ser Arg Glu Asp Glu His Thr His Thr Asn Ser Val Thr 130 135 140 Asn Ser Ser Ser Ile Val Asp Leu Pro Val His Gln Leu Ser Ser Pro 145 150 155 160 Phe Tyr Thr Lys Thr Thr Lys Met Lys Arg Lys Leu Asp His Gly Ser 165 170 175 Glu Val Arg Ser Phe Ser Leu Gly Lys Lys Pro Cys Lys Val Ser Glu 180 185 190 Tyr Thr Ser Thr Thr Gly Leu Val Pro Cys Ser Ala Thr Pro Thr Thr 195 200 205 Phe Gly Asp Leu Arg Ala Ala Asn Gly Gln Gly Gln Gln Arg Arg Arg 210 215 220 Ile Thr Ser Val Gln Pro Pro Thr Gly Leu Gln Glu Trp Leu Lys Met 225 230 235 240 Phe Gln Ser Trp Ser Gly Pro Glu Lys Leu Leu Ala Leu Asp Glu Leu 245 250 255 Ile Asp Ser Cys Glu Pro Thr Gln Val Lys His Met Met Gln Val Ile 260 265 270 Glu Pro Gln Phe Gln Arg Asp Phe Ile Ser Leu Leu Pro Lys Glu Leu 275 280 285 Ala Leu Tyr Val Leu Ser Phe Leu Glu Pro Lys Asp Leu Leu Gln Ala 290 295 300 Ala Gln Thr Cys Arg Tyr Trp Arg Ile Leu Ala Glu Asp Asn Leu Leu 305 310 315 320 Trp Arg Glu Lys Cys Lys Glu Glu Gly Ile Asp Glu Pro Leu His Ile 325 330 335 Lys Arg Arg Lys Val Ile Lys Pro Gly Phe Ile His Ser Pro Trp Lys 340 345 350 Ser Ala Tyr Ile Arg Gln His Arg Ile Asp Thr Asn Trp Arg Arg Gly 355 360 365 Glu Leu Lys Ser Pro Lys Val Leu Lys Gly His Asp Asp His Val Ile 370 375 380 Thr Cys Leu Gln Phe Cys Gly Asn Arg Ile Val Ser Gly Ser Asp Asp 385 390 395 400 Asn Thr Leu Lys Val Trp Ser Ala Val Thr Gly Lys Cys Leu Arg Thr 405 410 415 Leu Val Gly His Thr Gly Gly Val Trp Ser Ser Gln Met Arg Asp Asn 420 425 430 Ile Ile Ile Ser Gly Ser Thr Asp Arg Thr Leu Lys Val Trp Asn Ala 435 440 445 Glu Thr Gly Glu Cys Ile His Thr Leu Tyr Gly His Thr Ser Thr Val 450 455 460 Arg Cys Met His Leu His Glu Lys Arg Val Val Ser Gly Ser Arg Asp 465 470 475 480 Ala Thr Leu Arg Val Trp Asp Ile Glu Thr Gly Gln Cys Leu His Val 485 490 495 Leu Met Gly His Val Ala Ala Val Arg Cys Val Gln Tyr Asp Gly Arg 500 505 510 Arg Val Val Ser Gly Ala Tyr Asp Phe Met Val Lys Val Trp Asp Pro 515 520 525 Glu Thr Glu Thr Cys Leu His Thr Leu Gln Gly His Thr Asn Arg Val 530 535 540 Tyr Ser Leu Gln Phe Asp Gly Ile His Val Val Ser Gly Ser Leu Asp 545 550 555 560 Thr Ser Ile Arg Val Trp Asp Val Glu Thr Gly Asn Cys Ile His Thr 565 570 575 Leu Thr Gly His Gln Ser Leu Thr Ser Gly Met Glu Leu Lys Asp Asn 580 585 590 Ile Leu Val Ser Gly Asn Ala Asp Ser Thr Val Lys Ile Trp Asp Ile 595 600 605 Lys Thr Gly Gln Cys Leu Gln Thr Leu Gln Gly Pro Asn Lys His Gln 610 615 620 Ser Ala Val Thr Cys Leu Gln Phe Asn Lys Asn Phe Val Ile Thr Ser 625 630 635 640 Ser Asp Asp Gly Thr Val Lys Leu Trp Asp Leu Lys Thr Gly Glu Phe 645 650 655 Ile Arg Asn Leu Val Thr Leu Glu Ser Gly Gly Ser Gly Gly Val Val 660 665 670 Trp Arg Ile Arg Ala Ser Asn Thr Lys Leu Val Cys Ala Val Gly Ser 675 680 685 Arg Asn Gly Thr Glu Glu Thr Lys Leu Leu Val Leu Asp Phe Asp Val 690 695 700 Asp Met Lys 705 <210> SEQ ID NO 25 <211> LENGTH: 587 <212> TYPE: PRT <213> ORGANISM: Caenorhabditis elegans <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/AAC47809 <309> DATABASE ENTRY DATE: 1997-12-12 <313> RELEVANT RESIDUES: (1)..(587) <400> SEQUENCE: 25 Met Trp Pro Arg Asn Asp Val His Met Asp Asp Gly Ser Met Thr Pro 1 5 10 15 Glu Asp Gln Glu Pro Val Thr Asp Asn Asp Met Glu Tyr Asn Asp Asn 20 25 30 Gly Glu Glu Ser Ser Tyr Ser Asn Gly Ser Ser Ser Ser Tyr Asn Ala 35 40 45 Asp Lys Leu Ser Ser Ser Arg Pro Leu Gln His Lys Leu Asp Leu Ser 50 55 60 Ala Ser Pro Ser Arg Asn Asn Asp Leu Asn Pro Arg Val Glu His Leu 65 70 75 80 Ile Ala Leu Phe Lys Asp Leu Ser Ser Ala Glu Gln Met Asp Ala Phe 85 90 95 Thr Arg Leu Leu Gln Glu Ser Asn Met Thr Asn Ile Arg Gln Leu Arg 100 105 110 Ala Ile Ile Glu Pro His Phe Gln Arg Asp Phe Leu Ser Cys Leu Pro 115 120 125 Val Glu Leu Gly Met Lys Ile Leu His Asn Leu Thr Gly Tyr Asp Leu 130 135 140 Leu Lys Val Ala Gln Val Ser Lys Asn Trp Lys Leu Ile Ser Glu Ile 145 150 155 160 Asp Lys Ile Trp Lys Ser Leu Gly Val Glu Glu Phe Lys His His Pro 165 170 175 Asp Pro Thr Asp Arg Val Thr Gly Ala Trp Gln Gly Thr Ala Ile Ala 180 185 190 Ala Gly Val Thr Ile Pro Asp His Ile Gln Pro Cys Asp Leu Asn Val 195 200 205 His Arg Phe Leu Lys Leu Gln Lys Phe Gly Asp Ile Phe Glu Arg Ala 210 215 220 Ala Asp Lys Ser Arg Tyr Leu Arg Ala Asp Lys Ile Glu Lys Asn Trp 225 230 235 240 Asn Ala Asn Pro Ile Met Gly Ser Ala Val Leu Arg Gly His Glu Asp 245 250 255 His Val Ile Thr Cys Met Gln Ile His Asp Asp Val Leu Val Thr Gly 260 265 270 Ser Asp Asp Asn Thr Leu Lys Val Trp Cys Ile Asp Lys Gly Glu Val 275 280 285 Met Tyr Thr Leu Val Gly His Thr Gly Gly Val Trp Thr Ser Gln Ile 290 295 300 Ser Gln Cys Gly Arg Tyr Ile Val Ser Gly Ser Thr Asp Arg Thr Val 305 310 315 320 Lys Val Trp Ser Thr Val Asp Gly Ser Leu Leu His Thr Leu Gln Gly 325 330 335 His Thr Ser Thr Val Arg Cys Met Ala Met Ala Gly Ser Ile Leu Val 340 345 350 Thr Gly Ser Arg Asp Thr Thr Leu Arg Val Trp Asp Val Glu Ser Gly 355 360 365 Arg His Leu Ala Thr Leu His Gly His His Ala Ala Val Arg Cys Val 370 375 380 Gln Phe Asp Gly Thr Thr Val Val Ser Gly Gly Tyr Asp Phe Thr Val 385 390 395 400 Lys Ile Trp Asn Ala His Thr Gly Arg Cys Ile Arg Thr Leu Thr Gly 405 410 415 His Asn Asn Arg Val Tyr Ser Leu Leu Phe Glu Ser Glu Arg Ser Ile 420 425 430 Val Cys Ser Gly Ser Leu Asp Thr Ser Ile Arg Val Trp Asp Phe Thr 435 440 445 Arg Pro Glu Gly Gln Glu Cys Val Ala Leu Leu Gln Gly His Thr Ser 450 455 460 Leu Thr Ser Gly Met Gln Leu Arg Gly Asn Ile Leu Val Ser Cys Asn 465 470 475 480 Ala Asp Ser His Val Arg Val Trp Asp Ile His Glu Gly Thr Cys Val 485 490 495 His Met Leu Ser Gly His Arg Ser Ala Ile Thr Ser Leu Gln Trp Phe 500 505 510 Gly Arg Asn Met Val Ala Thr Ser Ser Asp Asp Gly Thr Val Lys Leu 515 520 525 Trp Asp Ile Glu Arg Gly Ala Leu Ile Arg Asp Leu Val Thr Leu Asp 530 535 540 Ser Gly Gly Asn Gly Gly Cys Ile Trp Arg Leu Cys Ser Thr Ser Thr 545 550 555 560 Met Leu Ala Cys Ala Val Gly Ser Arg Asn Asn Thr Glu Glu Thr Lys 565 570 575 Val Ile Leu Leu Asp Phe Asp Ala Val Tyr Pro 580 585 <210> SEQ ID NO 26 <211> LENGTH: 627 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/AAK57547 <309> DATABASE ENTRY DATE: 2001-08-22 <313> RELEVANT RESIDUES: (1)..(627) <400> SEQUENCE: 26 Met Cys Val Pro Arg Ser Gly Leu Ile Leu Ser Cys Ile Cys Leu Tyr 1 5 10 15 Cys Gly Val Leu Leu Pro Val Leu Leu Pro Asn Leu Pro Phe Leu Thr 20 25 30 Cys Leu Ser Met Ser Thr Leu Glu Ser Val Thr Tyr Leu Pro Glu Lys 35 40 45 Gly Leu Tyr Cys Gln Arg Leu Pro Ser Ser Arg Thr His Gly Gly Thr 50 55 60 Glu Ser Leu Lys Gly Lys Asn Thr Glu Asn Met Gly Phe Tyr Gly Thr 65 70 75 80 Leu Lys Met Ile Phe Tyr Lys Met Lys Arg Lys Leu Asp His Gly Ser 85 90 95 Glu Val Arg Ser Phe Ser Leu Gly Lys Lys Pro Cys Lys Val Ser Glu 100 105 110 Tyr Thr Ser Thr Thr Gly Leu Val Pro Cys Ser Ala Thr Pro Thr Thr 115 120 125 Phe Gly Asp Leu Arg Ala Ala Asn Gly Gln Gly Gln Gln Arg Arg Arg 130 135 140 Ile Thr Ser Val Gln Pro Pro Thr Gly Leu Gln Glu Trp Leu Lys Met 145 150 155 160 Phe Gln Ser Trp Ser Gly Pro Glu Lys Leu Leu Ala Leu Asp Glu Leu 165 170 175 Ile Asp Ser Cys Glu Pro Thr Gln Val Lys His Met Met Gln Val Ile 180 185 190 Glu Pro Gln Phe Gln Arg Asp Phe Ile Ser Leu Leu Pro Lys Glu Leu 195 200 205 Ala Leu Tyr Val Leu Ser Phe Leu Glu Pro Lys Asp Leu Leu Gln Ala 210 215 220 Ala Gln Thr Cys Arg Tyr Trp Arg Ile Leu Ala Glu Asp Asn Leu Leu 225 230 235 240 Trp Arg Glu Lys Cys Lys Glu Glu Gly Ile Asp Glu Pro Leu His Ile 245 250 255 Lys Arg Arg Lys Val Ile Lys Pro Gly Phe Ile His Ser Pro Trp Lys 260 265 270 Ser Ala Tyr Ile Arg Gln His Arg Ile Asp Thr Asn Trp Arg Arg Gly 275 280 285 Glu Leu Lys Ser Pro Lys Val Leu Lys Gly His Asp Asp His Val Ile 290 295 300 Thr Cys Leu Gln Phe Cys Gly Asn Arg Ile Val Ser Gly Ser Asp Asp 305 310 315 320 Asn Thr Leu Lys Val Trp Ser Ala Val Thr Gly Lys Cys Leu Arg Thr 325 330 335 Leu Val Gly His Thr Gly Gly Val Trp Ser Ser Gln Met Arg Asp Asn 340 345 350 Ile Ile Ile Ser Gly Ser Thr Asp Arg Thr Leu Lys Val Trp Asn Ala 355 360 365 Glu Thr Gly Glu Cys Ile His Thr Leu Tyr Gly His Thr Ser Thr Val 370 375 380 Arg Cys Met His Leu His Glu Lys Arg Val Val Ser Gly Ser Arg Asp 385 390 395 400 Ala Thr Leu Arg Val Trp Asp Ile Glu Thr Gly Gln Cys Leu His Val 405 410 415 Leu Met Gly His Val Ala Ala Val Arg Cys Val Gln Tyr Asp Gly Arg 420 425 430 Arg Val Val Ser Gly Ala Tyr Asp Phe Met Val Lys Val Trp Asp Pro 435 440 445 Glu Thr Glu Thr Cys Leu His Thr Leu Gln Gly His Thr Asn Arg Val 450 455 460 Tyr Ser Leu Gln Phe Asp Gly Ile His Val Val Ser Gly Ser Leu Asp 465 470 475 480 Thr Ser Ile Arg Val Trp Asp Val Glu Thr Gly Asn Cys Ile His Thr 485 490 495 Leu Thr Gly His Gln Ser Leu Thr Ser Gly Met Glu Leu Lys Asp Asn 500 505 510 Ile Leu Val Ser Gly Asn Ala Asp Ser Thr Val Lys Ile Trp Asp Ile 515 520 525 Lys Thr Gly Gln Cys Leu Gln Thr Leu Gln Gly Pro Asn Lys His Gln 530 535 540 Ser Ala Val Thr Cys Leu Gln Phe Asn Lys Asn Phe Val Ile Thr Ser 545 550 555 560 Ser Asp Asp Gly Thr Val Lys Leu Trp Asp Leu Lys Thr Gly Glu Phe 565 570 575 Ile Arg Asn Leu Val Thr Leu Glu Ser Gly Gly Ser Gly Gly Val Val 580 585 590 Trp Arg Ile Arg Ala Ser Asn Thr Lys Leu Val Cys Ala Val Gly Ser 595 600 605 Arg Asn Gly Thr Glu Glu Thr Lys Leu Leu Val Leu Asp Phe Asp Val 610 615 620 Asp Met Lys 625 <210> SEQ ID NO 27 <211> LENGTH: 224 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <400> SEQUENCE: 27 Met Ala Val Gly Asn Ile Asn Glu Leu Pro Glu Asn Ile Leu Leu Glu 1 5 10 15 Leu Phe Thr His Val Pro Ala Arg Gln Leu Leu Leu Asn Cys Arg Leu 20 25 30 Val Cys Ser Leu Trp Arg Asp Leu Ile Asp Leu Val Thr Leu Trp Lys 35 40 45 Arg Lys Cys Leu Arg Glu Gly Phe Ile Thr Glu Asp Trp Asp Gln Pro 50 55 60 Val Ala Asp Trp Lys Ile Phe Tyr Phe Leu Arg Ser Leu His Arg Asn 65 70 75 80 Leu Leu His Asn Pro Cys Ala Glu Glu Gly Phe Glu Phe Trp Ser Leu 85 90 95 Asp Val Asn Gly Gly Asp Glu Trp Lys Val Glu Asp Leu Ser Arg Asp 100 105 110 Gln Arg Lys Glu Phe Pro Asn Asp Gln Val Arg Ser Gln Ala Arg Leu 115 120 125 Arg Val Gln Val Pro Ala Val Arg Ser Ala Pro Val Val Arg Ala Arg 130 135 140 Ala Ser Gly Asp Leu Pro Ala Arg Pro Gly Asp His Pro Ala Glu Glu 145 150 155 160 Arg Cys Gln Val Glu Gly Gly Leu Pro His Ile Leu Gln Leu Pro Ala 165 170 175 Arg Arg Pro Leu His Leu Val Ser Ala Arg Arg Arg Gly His Ser Leu 180 185 190 Leu Gly Arg Leu Val Arg Pro Glu Gly His Gln Gln Gln His His His 195 200 205 Arg Ala Pro Ala Ala Leu Thr Pro Pro Glu Pro Pro Ser Ala Glu Pro 210 215 220 <210> SEQ ID NO 28 <211> LENGTH: 815 <212> TYPE: PRT <213> ORGANISM: Saccharomyces cerevisiae <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/AAB38821 <309> DATABASE ENTRY DATE: 1996-12-17 <313> RELEVANT RESIDUES: (1)..(815) <400> SEQUENCE: 28 Met Ser Glu Thr Leu Pro Arg Ser Asp Asp Leu Glu Ala Thr Trp Asn 1 5 10 15 Phe Ile Glu Pro Gly Ile Asn Gln Ile Leu Gly Asn Glu Lys Asn Gln 20 25 30 Ala Ser Thr Ser Lys Arg Val Tyr Lys Ile Leu Ser Pro Thr Met Tyr 35 40 45 Met Glu Val Tyr Thr Ala Ile Tyr Asn Tyr Cys Val Asn Lys Ser Arg 50 55 60 Ser Ser Gly His Phe Ser Thr Asp Ser Arg Thr Gly Gln Ser Thr Ile 65 70 75 80 Leu Val Gly Ser Glu Ile Tyr Glu Lys Leu Lys Asn Tyr Leu Lys Asn 85 90 95 Tyr Ile Leu Asn Phe Lys Gln Ser Asn Ser Glu Thr Phe Leu Gln Phe 100 105 110 Tyr Val Lys Arg Trp Lys Arg Phe Thr Ile Gly Ala Ile Phe Leu Asn 115 120 125 His Ala Phe Asp Tyr Met Asn Arg Tyr Trp Val Gln Lys Glu Arg Ser 130 135 140 Asp Gly Lys Arg His Ile Phe Asp Val Asn Thr Leu Cys Leu Met Thr 145 150 155 160 Trp Lys Glu Val Met Phe Asp Pro Ser Lys Asp Val Leu Ile Asn Glu 165 170 175 Leu Leu Asp Gln Val Thr Leu Gly Arg Glu Gly Gln Ile Ile Gln Arg 180 185 190 Ser Asn Ile Ser Thr Ala Ile Lys Ser Leu Val Ala Leu Gly Ile Asp 195 200 205 Pro Gln Asp Leu Lys Lys Leu Asn Leu Asn Val Tyr Ile Gln Val Phe 210 215 220 Glu Lys Pro Phe Leu Lys Lys Thr Gln Glu Tyr Tyr Thr Gln Tyr Thr 225 230 235 240 Asn Asp Tyr Leu Glu Lys His Ser Val Thr Glu Tyr Ile Phe Glu Ala 245 250 255 His Glu Ile Ile Lys Arg Glu Glu Lys Ala Met Thr Ile Tyr Trp Asp 260 265 270 Asp His Thr Lys Lys Pro Leu Ser Met Ala Leu Asn Lys Val Leu Ile 275 280 285 Thr Asp His Ile Glu Lys Leu Glu Asn Glu Phe Val Val Leu Leu Asp 290 295 300 Ala Arg Asp Ile Glu Lys Ile Thr Ser Leu Tyr Ala Leu Ile Arg Arg 305 310 315 320 Asp Phe Thr Leu Ile Pro Arg Met Ala Ser Val Phe Glu Asn Tyr Val 325 330 335 Lys Lys Thr Gly Glu Asn Glu Ile Ser Ser Leu Leu Ala Met His Lys 340 345 350 His Asn Ile Met Lys Asn Glu Asn Ala Asn Pro Lys Lys Leu Ala Leu 355 360 365 Met Thr Ala His Ser Leu Ser Pro Lys Asp Tyr Ile Lys Lys Leu Leu 370 375 380 Glu Val His Asp Ile Phe Ser Lys Ile Phe Asn Glu Ser Phe Pro Asp 385 390 395 400 Asp Ile Pro Leu Ala Lys Ala Leu Asp Asn Ala Cys Gly Ala Phe Ile 405 410 415 Asn Ile Asn Glu Phe Ala Leu Pro Ala Gly Ser Pro Lys Ser Ala Thr 420 425 430 Ser Lys Thr Ser Glu Met Leu Ala Lys Tyr Ser Asp Ile Leu Leu Lys 435 440 445 Lys Ala Thr Lys Pro Glu Val Ala Ser Asp Met Ser Asp Glu Asp Ile 450 455 460 Ile Thr Ile Phe Lys Tyr Leu Thr Asp Lys Asp Ala Phe Glu Thr His 465 470 475 480 Tyr Arg Arg Leu Phe Ala Lys Arg Leu Ile His Gly Thr Ser Thr Ser 485 490 495 Ala Glu Asp Glu Glu Asn Ile Ile Gln Arg Leu Gln Ala Ala Asn Ser 500 505 510 Met Glu Tyr Thr Gly Lys Ile Thr Lys Met Phe Gln Asp Ile Arg Leu 515 520 525 Ser Lys Ile Leu Glu Asp Asp Phe Ala Val Ala Leu Lys Asn Glu Pro 530 535 540 Asp Tyr Ser Lys Ala Lys Tyr Pro Asp Leu Gln Pro Phe Val Leu Ala 545 550 555 560 Glu Asn Met Trp Pro Phe Ser Tyr Gln Glu Val Glu Phe Lys Leu Pro 565 570 575 Lys Glu Leu Val Pro Ser His Glu Lys Leu Lys Glu Ser Tyr Ser Gln 580 585 590 Lys His Asn Gly Arg Ile Leu Lys Trp Leu Trp Pro Leu Cys Arg Gly 595 600 605 Glu Leu Lys Ala Asp Ile Gly Lys Pro Gly Arg Met Pro Phe Asn Phe 610 615 620 Thr Val Thr Leu Phe Gln Met Ala Ile Leu Leu Leu Tyr Asn Asp Ala 625 630 635 640 Asp Val Leu Thr Leu Glu Asn Ile Gln Glu Gly Thr Ser Leu Thr Ile 645 650 655 Gln His Ile Ala Ala Ala Met Val Pro Phe Ile Lys Phe Lys Leu Ile 660 665 670 Gln Gln Val Pro Pro Gly Leu Asp Ala Leu Val Lys Pro Glu Thr Gln 675 680 685 Phe Lys Leu Ser Arg Pro Tyr Lys Ala Leu Lys Thr Asn Ile Asn Phe 690 695 700 Ala Ser Gly Val Lys Asn Asp Ile Leu Gln Ser Leu Ser Gly Gly Gly 705 710 715 720 His Asp Asn His Gly Asn Lys Leu Gly Asn Lys Arg Leu Thr Glu Asp 725 730 735 Glu Arg Ile Glu Lys Glu Leu Asn Thr Glu Arg Gln Ile Phe Leu Glu 740 745 750 Ala Cys Ile Val Arg Ile Met Lys Ala Lys Arg Asn Leu Pro His Thr 755 760 765 Thr Leu Val Asn Glu Cys Ile Ala Gln Ser His Gln Arg Phe Asn Ala 770 775 780 Lys Val Ser Met Val Lys Arg Ala Ile Asp Ser Leu Ile Gln Lys Gly 785 790 795 800 Tyr Leu Gln Arg Gly Asp Asp Gly Glu Ser Tyr Ala Tyr Leu Ala 805 810 815 <210> SEQ ID NO 29 <211> LENGTH: 768 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/AAC36304 <309> DATABASE ENTRY DATE: 1998-09-19 <313> RELEVANT RESIDUES: (1)..(768) <400> SEQUENCE: 29 Met Ser Asn Leu Ser Lys Gly Thr Gly Ser Arg Lys Asp Thr Lys Met 1 5 10 15 Arg Ile Arg Ala Phe Pro Met Thr Met Asp Glu Lys Tyr Val Asn Ser 20 25 30 Ile Trp Asp Leu Leu Lys Asn Ala Ile Gln Glu Ile Gln Arg Lys Asn 35 40 45 Asn Ser Gly Leu Ser Phe Glu Glu Leu Tyr Arg Asn Ala Tyr Thr Met 50 55 60 Val Leu His Lys His Gly Glu Lys Leu Tyr Thr Gly Leu Arg Glu Val 65 70 75 80 Val Thr Glu His Leu Ile Asn Lys Val Arg Glu Asp Val Leu Asn Ser 85 90 95 Leu Asn Asn Asn Phe Leu Gln Thr Leu Asn Gln Ala Trp Asn Asp His 100 105 110 Gln Thr Ala Met Val Met Ile Arg Asp Ile Leu Met Tyr Met Asp Arg 115 120 125 Val Tyr Val Gln Gln Asn Asn Val Glu Asn Val Tyr Asn Leu Gly Leu 130 135 140 Ile Ile Phe Arg Asp Gln Val Val Arg Tyr Gly Cys Ile Arg Asp His 145 150 155 160 Leu Arg Gln Thr Leu Leu Asp Met Ile Ala Arg Glu Arg Lys Gly Glu 165 170 175 Val Val Asp Arg Gly Ala Ile Arg Asn Ala Cys Gln Met Leu Met Ile 180 185 190 Leu Gly Leu Glu Gly Arg Ser Val Tyr Glu Glu Asp Phe Glu Ala Pro 195 200 205 Phe Leu Glu Met Ser Ala Glu Phe Phe Gln Met Glu Ser Gln Lys Phe 210 215 220 Leu Ala Glu Asn Ser Ala Ser Val Tyr Ile Lys Lys Val Glu Ala Arg 225 230 235 240 Ile Asn Glu Glu Ile Glu Arg Val Met His Cys Leu Asp Lys Ser Thr 245 250 255 Glu Glu Pro Ile Val Lys Val Val Glu Arg Glu Leu Ile Ser Lys His 260 265 270 Met Lys Thr Ile Val Glu Met Glu Asn Ser Gly Leu Val His Met Leu 275 280 285 Lys Asn Gly Lys Thr Glu Asp Leu Gly Cys Met Tyr Lys Leu Phe Ser 290 295 300 Arg Val Pro Asn Gly Leu Lys Thr Met Cys Glu Cys Met Ser Ser Tyr 305 310 315 320 Leu Arg Glu Gln Gly Lys Ala Leu Val Ser Glu Glu Gly Glu Gly Lys 325 330 335 Asn Pro Val Asp Tyr Ile Gln Gly Leu Leu Asp Leu Lys Ser Arg Phe 340 345 350 Asp Arg Phe Leu Leu Glu Ser Phe Asn Asn Asp Arg Leu Phe Lys Gln 355 360 365 Thr Ile Ala Gly Asp Phe Glu Tyr Phe Leu Asn Leu Asn Ser Arg Ser 370 375 380 Pro Glu Tyr Leu Ser Leu Phe Ile Asp Asp Lys Leu Lys Lys Gly Val 385 390 395 400 Lys Gly Leu Thr Glu Gln Glu Val Glu Thr Ile Leu Asp Lys Ala Met 405 410 415 Val Leu Phe Arg Phe Met Gln Glu Lys Asp Val Phe Glu Arg Tyr Tyr 420 425 430 Lys Gln His Leu Ala Arg Arg Leu Leu Thr Asn Lys Ser Val Ser Asp 435 440 445 Asp Ser Glu Lys Asn Met Ile Ser Lys Leu Lys Thr Glu Cys Gly Cys 450 455 460 Gln Phe Thr Ser Lys Leu Glu Gly Met Phe Arg Asp Met Ser Ile Ser 465 470 475 480 Asn Thr Thr Met Asp Glu Phe Arg Gln His Leu Gln Ala Thr Gly Val 485 490 495 Ser Leu Gly Gly Val Asp Leu Thr Val Arg Val Leu Thr Thr Gly Tyr 500 505 510 Trp Pro Thr Gln Ser Ala Thr Pro Lys Cys Asn Ile Pro Pro Ala Pro 515 520 525 Arg His Ala Phe Glu Ile Phe Arg Arg Phe Tyr Leu Ala Lys His Ser 530 535 540 Gly Arg Gln Leu Thr Leu Gln His His Met Gly Ser Ala Asp Leu Asn 545 550 555 560 Ala Thr Phe Tyr Gly Pro Val Lys Lys Glu Asp Gly Ser Glu Val Gly 565 570 575 Val Gly Gly Ala Gln Val Thr Gly Ser Asn Thr Arg Lys His Ile Leu 580 585 590 Gln Val Ser Thr Phe Gln Met Thr Ile Leu Met Leu Phe Asn Asn Arg 595 600 605 Glu Lys Tyr Thr Phe Glu Glu Ile Gln Gln Glu Thr Asp Ile Pro Glu 610 615 620 Arg Glu Leu Val Arg Ala Leu Gln Ser Leu Ala Cys Gly Lys Pro Thr 625 630 635 640 Gln Arg Val Leu Thr Lys Glu Pro Lys Ser Lys Glu Ile Glu Asn Gly 645 650 655 His Ile Phe Thr Val Asn Asp Gln Phe Thr Ser Lys Leu His Arg Val 660 665 670 Lys Ile Gln Thr Val Ala Ala Lys Gln Gly Glu Ser Asp Pro Glu Arg 675 680 685 Lys Glu Thr Arg Gln Lys Val Asp Asp Asp Arg Lys His Glu Ile Glu 690 695 700 Ala Ala Ile Val Arg Ile Met Lys Ser Arg Lys Lys Met Gln His Asn 705 710 715 720 Val Leu Val Ala Glu Val Thr Gln Gln Leu Lys Ala Arg Phe Leu Pro 725 730 735 Ser Pro Val Val Ile Lys Lys Arg Ile Glu Gly Leu Ile Glu Arg Glu 740 745 750 Tyr Leu Ala Arg Thr Pro Glu Asp Arg Lys Val Tyr Thr Tyr Val Ala 755 760 765 <210> SEQ ID NO 30 <211> LENGTH: 745 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/ AAC51190 <309> DATABASE ENTRY DATE: 1997-04-03 <313> RELEVANT RESIDUES: (1)..(745) <400> SEQUENCE: 30 Met Ser Leu Lys Pro Arg Val Val Asp Phe Asp Glu Thr Trp Asn Lys 1 5 10 15 Leu Leu Thr Thr Ile Lys Ala Val Val Met Leu Glu Tyr Val Glu Arg 20 25 30 Ala Thr Trp Asn Asp Arg Phe Ser Asp Ile Tyr Ala Leu Cys Val Ala 35 40 45 Tyr Pro Glu Pro Leu Gly Glu Arg Leu Tyr Thr Glu Thr Lys Ile Phe 50 55 60 Leu Glu Asn His Val Arg His Leu His Lys Arg Val Leu Glu Ser Glu 65 70 75 80 Glu Gln Val Leu Val Met Tyr His Arg Tyr Trp Glu Glu Tyr Ser Lys 85 90 95 Gly Ala Asp Tyr Met Asp Cys Leu Tyr Arg Tyr Leu Ser Thr Gln Phe 100 105 110 Ile Lys Lys Asn Lys Leu Thr Glu Ala Asp Leu Gln Tyr Gly Tyr Gly 115 120 125 Gly Val Asp Met Asn Glu Pro Leu Met Glu Ile Gly Glu Leu Ala Leu 130 135 140 Asp Met Trp Arg Lys Leu Met Val Glu Pro Leu Gln Ala Ile Leu Ile 145 150 155 160 Arg Met Leu Leu Arg Glu Ile Lys Asn Asp Arg Gly Gly Glu Asp Pro 165 170 175 Asn Gln Lys Val Ile His Gly Val Ile Asn Ser Phe Val His Val Glu 180 185 190 Gln Tyr Lys Lys Lys Phe Pro Leu Lys Phe Tyr Gln Glu Ile Phe Glu 195 200 205 Ser Pro Phe Leu Thr Glu Thr Gly Glu Tyr Tyr Lys Gln Glu Ala Ser 210 215 220 Asn Leu Leu Gln Glu Ser Asn Cys Ser Gln Tyr Met Glu Lys Val Leu 225 230 235 240 Gly Arg Leu Lys Asp Glu Glu Ile Arg Cys Arg Lys Tyr Leu His Pro 245 250 255 Ser Ser Tyr Thr Lys Val Ile His Glu Cys Gln Gln Arg Met Val Ala 260 265 270 Asp His Leu Gln Phe Leu His Ala Glu Cys His Asn Ile Ile Arg Gln 275 280 285 Glu Lys Lys Asn Asp Met Ala Asn Met Tyr Val Leu Leu Arg Ala Val 290 295 300 Ser Thr Gly Leu Pro His Met Ile Gln Glu Leu Gln Asn His Ile His 305 310 315 320 Asp Glu Gly Leu Arg Ala Thr Ser Asn Leu Thr Gln Glu Asn Met Pro 325 330 335 Thr Leu Phe Val Glu Ser Val Leu Glu Val His Gly Lys Phe Val Gln 340 345 350 Leu Ile Asn Thr Val Leu Asn Gly Asp Gln His Phe Met Ser Ala Leu 355 360 365 Asp Lys Ala Leu Thr Ser Val Val Asn Tyr Arg Glu Pro Lys Ser Val 370 375 380 Cys Lys Ala Pro Glu Leu Leu Ala Lys Tyr Cys Asp Asn Leu Leu Lys 385 390 395 400 Lys Ser Ala Lys Gly Met Thr Glu Asn Glu Val Glu Asp Arg Leu Thr 405 410 415 Ser Phe Ile Thr Val Phe Lys Tyr Ile Asp Asp Lys Asp Val Phe Gln 420 425 430 Lys Phe Tyr Ala Arg Met Leu Ala Lys Arg Leu Ile His Gly Leu Ser 435 440 445 Met Ser Met Asp Ser Glu Glu Ala Met Ile Asn Lys Leu Lys Gln Ala 450 455 460 Cys Gly Tyr Glu Phe Thr Ser Lys Leu His Arg Met Tyr Thr Asp Met 465 470 475 480 Ser Val Ser Ala Asp Leu Asn Asn Lys Phe Asn Asn Phe Ile Lys Asn 485 490 495 Gln Asp Thr Val Ile Asp Leu Gly Ile Ser Phe Gln Ile Tyr Val Leu 500 505 510 Gln Ala Gly Ala Trp Pro Leu Thr Gln Ala Pro Ser Ser Thr Phe Ala 515 520 525 Ile Pro Gln Glu Leu Glu Lys Ser Val Gln Met Phe Glu Leu Phe Tyr 530 535 540 Ser Gln His Phe Ser Gly Arg Lys Leu Thr Trp Leu His Tyr Leu Cys 545 550 555 560 Thr Gly Glu Val Lys Met Asn Tyr Leu Gly Lys Pro Tyr Val Ala Met 565 570 575 Val Thr Thr Tyr Gln Met Ala Val Leu Leu Ala Phe Asn Asn Ser Glu 580 585 590 Thr Val Ser Tyr Lys Glu Leu Gln Asp Ser Thr Gln Met Asn Glu Lys 595 600 605 Glu Leu Thr Lys Thr Ile Lys Ser Leu Leu Asp Val Lys Met Ile Asn 610 615 620 His Asp Ser Glu Lys Glu Asp Ile Asp Ala Glu Ser Ser Phe Ser Leu 625 630 635 640 Asn Met Asn Phe Ser Ser Lys Arg Thr Lys Phe Lys Ile Thr Thr Ser 645 650 655 Met Gln Lys Asp Thr Pro Gln Glu Met Glu Gln Thr Arg Ser Ala Val 660 665 670 Asp Glu Asp Arg Lys Met Tyr Leu Gln Ala Ala Ile Val Arg Ile Met 675 680 685 Lys Ala Arg Lys Val Leu Arg His Asn Ala Leu Ile Gln Glu Val Ile 690 695 700 Ser Gln Ser Arg Ala Arg Phe Asn Pro Ser Ile Ser Met Ile Lys Lys 705 710 715 720 Cys Ile Glu Val Leu Ile Asp Lys Gln Tyr Ile Glu Arg Ser Gln Ala 725 730 735 Ser Ala Asp Glu Tyr Ser Tyr Val Ala 740 745 <210> SEQ ID NO 31 <211> LENGTH: 768 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <400> SEQUENCE: 31 Met Ser Asn Leu Ser Lys Gly Thr Gly Ser Arg Lys Asp Thr Lys Met 1 5 10 15 Arg Ile Arg Ala Phe Pro Met Thr Met Asp Glu Lys Tyr Val Asn Ser 20 25 30 Ile Trp Asp Leu Leu Lys Asn Ala Ile Gln Glu Ile Gln Arg Lys Asn 35 40 45 Asn Ser Gly Leu Ser Phe Glu Glu Leu Tyr Arg Asn Ala Tyr Thr Met 50 55 60 Val Leu His Lys His Gly Glu Lys Leu Tyr Thr Gly Leu Arg Glu Val 65 70 75 80 Val Thr Glu His Leu Ile Asn Lys Val Arg Glu Asp Val Leu Asn Ser 85 90 95 Leu Asn Asn Asn Phe Leu Gln Thr Leu Asn Gln Ala Trp Asn Asp His 100 105 110 Gln Thr Ala Met Val Met Ile Arg Asp Ile Leu Met Tyr Met Asp Arg 115 120 125 Val Tyr Val Gln Gln Asn Asn Val Glu Asn Val Tyr Asn Leu Gly Leu 130 135 140 Ile Ile Phe Arg Asp Gln Val Val Arg Tyr Gly Cys Ile Arg Asp His 145 150 155 160 Leu Arg Gln Thr Leu Leu Asp Met Ile Ala Arg Glu Arg Lys Gly Glu 165 170 175 Val Val Asp Arg Gly Ala Ile Arg Asn Ala Cys Gln Met Leu Met Ile 180 185 190 Leu Gly Leu Glu Gly Arg Ser Val Tyr Glu Glu Asp Phe Glu Ala Pro 195 200 205 Phe Leu Glu Met Ser Ala Glu Phe Phe Gln Met Glu Ser Gln Lys Phe 210 215 220 Leu Ala Glu Asn Ser Ala Ser Val Tyr Ile Lys Lys Val Glu Ala Arg 225 230 235 240 Ile Asn Glu Glu Ile Glu Arg Val Met His Cys Leu Asp Lys Ser Thr 245 250 255 Glu Glu Pro Ile Val Lys Val Val Glu Arg Glu Leu Ile Ser Lys His 260 265 270 Met Lys Thr Ile Val Glu Met Glu Asn Ser Gly Leu Val His Met Leu 275 280 285 Lys Asn Gly Lys Thr Glu Asp Leu Gly Cys Met Tyr Lys Leu Phe Ser 290 295 300 Arg Val Pro Asn Gly Leu Lys Thr Met Cys Glu Cys Met Ser Ser Tyr 305 310 315 320 Leu Arg Glu Gln Gly Lys Ala Leu Val Ser Glu Glu Gly Glu Gly Lys 325 330 335 Asn Pro Val Asp Tyr Ile Gln Gly Leu Leu Asp Leu Lys Ser Arg Phe 340 345 350 Asp Arg Phe Leu Leu Glu Ser Phe Asn Asn Asp Arg Leu Phe Lys Gln 355 360 365 Thr Ile Ala Gly Asp Phe Glu Tyr Phe Leu Asn Leu Asn Ser Arg Ser 370 375 380 Pro Glu Tyr Leu Ser Leu Phe Ile Asp Asp Lys Leu Lys Lys Gly Val 385 390 395 400 Lys Gly Leu Thr Glu Gln Glu Val Glu Thr Ile Leu Asp Lys Ala Met 405 410 415 Val Leu Phe Arg Phe Met Gln Glu Lys Asp Val Phe Glu Arg Tyr Tyr 420 425 430 Lys Gln His Leu Ala Arg Arg Leu Leu Thr Asn Lys Ser Val Ser Asp 435 440 445 Asp Ser Glu Lys Asn Met Ile Ser Lys Leu Lys Thr Glu Cys Gly Cys 450 455 460 Gln Phe Thr Ser Lys Leu Glu Gly Met Phe Arg Asp Met Ser Ile Ser 465 470 475 480 Asn Thr Thr Met Asp Glu Phe Arg Gln His Leu Gln Ala Thr Gly Val 485 490 495 Ser Leu Gly Gly Val Asp Leu Thr Val Arg Val Leu Thr Thr Gly Tyr 500 505 510 Trp Pro Thr Gln Ser Ala Thr Pro Lys Cys Asn Ile Pro Pro Ala Pro 515 520 525 Arg His Ala Phe Glu Ile Phe Arg Arg Phe Tyr Leu Ala Lys His Ser 530 535 540 Gly Arg Gln Leu Thr Leu Gln His His Met Gly Ser Ala Asp Leu Asn 545 550 555 560 Ala Thr Phe Tyr Gly Pro Val Lys Lys Glu Asp Gly Ser Glu Val Gly 565 570 575 Val Gly Gly Ala Gln Val Thr Gly Ser Asn Thr Arg Lys His Ile Leu 580 585 590 Gln Val Ser Thr Phe Gln Met Thr Ile Leu Met Leu Phe Asn Asn Arg 595 600 605 Glu Lys Tyr Thr Phe Glu Glu Ile Gln Gln Glu Thr Asp Ile Pro Glu 610 615 620 Arg Glu Leu Val Arg Ala Leu Gln Ser Leu Ala Cys Gly Lys Pro Thr 625 630 635 640 Gln Arg Val Leu Thr Lys Glu Pro Lys Ser Lys Glu Ile Glu Asn Gly 645 650 655 His Ile Phe Thr Val Asn Asp Gln Phe Thr Ser Lys Leu His Arg Val 660 665 670 Lys Ile Gln Thr Val Ala Ala Lys Gln Gly Glu Ser Asp Pro Glu Arg 675 680 685 Lys Glu Thr Arg Gln Lys Val Asp Asp Asp Arg Lys His Glu Ile Glu 690 695 700 Ala Ala Ile Val Arg Ile Met Lys Ser Arg Lys Lys Met Gln His Asn 705 710 715 720 Val Leu Val Ala Glu Val Thr Gln Gln Leu Lys Ala Arg Phe Leu Pro 725 730 735 Ser Pro Val Val Ile Lys Lys Arg Ile Glu Gly Leu Ile Glu Arg Glu 740 745 750 Tyr Leu Ala Arg Thr Pro Glu Asp Arg Lys Val Tyr Thr Tyr Val Ala 755 760 765 <210> SEQ ID NO 32 <211> LENGTH: 745 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/ AAD23581 <309> DATABASE ENTRY DATE: 1999-04-06 <313> RELEVANT RESIDUES: (1)..(745) <400> SEQUENCE: 32 Met Ser Leu Lys Pro Arg Val Val Asp Phe Asp Glu Thr Trp Asn Lys 1 5 10 15 Leu Leu Thr Thr Ile Lys Ala Val Val Met Leu Glu Tyr Val Glu Arg 20 25 30 Ala Thr Trp Asn Asp Arg Phe Ser Asp Ile Tyr Ala Leu Cys Val Ala 35 40 45 Tyr Pro Glu Pro Leu Gly Glu Arg Leu Tyr Thr Glu Thr Lys Ile Phe 50 55 60 Leu Glu Asn His Val Arg His Leu His Lys Arg Val Leu Glu Ser Glu 65 70 75 80 Glu Gln Val Leu Val Met Tyr His Arg Tyr Trp Glu Glu Tyr Ser Lys 85 90 95 Gly Ala Asp Tyr Met Asp Cys Leu Tyr Arg Tyr Leu Asn Thr Gln Phe 100 105 110 Ile Lys Lys Asn Lys Leu Thr Glu Ala Asp Leu Gln Tyr Gly Tyr Gly 115 120 125 Gly Val Asp Met Asn Glu Pro Leu Met Glu Ile Gly Glu Leu Ala Leu 130 135 140 Asp Met Trp Arg Lys Leu Met Val Glu Pro Leu Gln Ala Ile Leu Ile 145 150 155 160 Arg Met Leu Leu Arg Glu Ile Lys Asn Asp Arg Gly Gly Glu Asp Pro 165 170 175 Asn Gln Lys Val Ile His Gly Val Ile Asn Ser Phe Val His Val Glu 180 185 190 Gln Tyr Lys Lys Lys Phe Pro Leu Lys Phe Tyr Gln Glu Ile Phe Glu 195 200 205 Ser Pro Phe Leu Thr Glu Thr Gly Glu Tyr Tyr Lys Gln Glu Ala Ser 210 215 220 Asn Leu Leu Gln Glu Ser Asn Cys Ser Gln Tyr Met Glu Lys Val Leu 225 230 235 240 Gly Arg Leu Lys Asp Glu Glu Ile Arg Cys Arg Lys Tyr Leu His Pro 245 250 255 Ser Ser Tyr Thr Lys Val Ile His Glu Cys Gln Gln Arg Met Val Ala 260 265 270 Asp His Leu Gln Phe Leu His Ala Glu Cys His Asn Ile Ile Arg Gln 275 280 285 Glu Lys Lys Asn Asp Met Ala Asn Met Tyr Val Leu Leu Arg Ala Val 290 295 300 Ser Thr Gly Leu Pro His Met Ile Gln Glu Leu Gln Asn His Ile His 305 310 315 320 Asp Glu Gly Leu Arg Ala Thr Ser Asn Leu Thr Gln Glu Asn Met Pro 325 330 335 Thr Leu Phe Val Glu Ser Val Leu Glu Val His Gly Lys Phe Val Gln 340 345 350 Leu Ile Asn Thr Val Leu Asn Gly Asp Gln His Phe Met Ser Ala Leu 355 360 365 Asp Lys Ala Leu Thr Ser Val Val Asn Tyr Arg Glu Pro Lys Ser Val 370 375 380 Cys Lys Ala Pro Glu Leu Leu Ala Lys Tyr Cys Asp Asn Leu Leu Lys 385 390 395 400 Lys Ser Ala Lys Gly Met Thr Glu Asn Glu Val Glu Asp Arg Leu Thr 405 410 415 Ser Phe Ile Thr Val Phe Lys Tyr Ile Asp Asp Lys Asp Val Phe Gln 420 425 430 Lys Phe Tyr Ala Arg Met Leu Ala Lys Arg Leu Ile His Gly Leu Ser 435 440 445 Met Ser Met Asp Ser Glu Glu Ala Met Ile Asn Lys Leu Lys Gln Ala 450 455 460 Cys Gly Tyr Glu Phe Thr Ser Lys Leu His Arg Met Tyr Thr Asp Met 465 470 475 480 Ser Val Ser Ala Asp Leu Asn Asn Lys Phe Asn Asn Phe Ile Lys Asn 485 490 495 Gln Asp Thr Val Ile Asp Leu Gly Ile Ser Phe Gln Ile Tyr Val Leu 500 505 510 Gln Ala Gly Ala Trp Pro Leu Thr Gln Ala Pro Ser Ser Thr Phe Ala 515 520 525 Ile Pro Gln Glu Leu Glu Lys Ser Val Gln Met Phe Glu Leu Phe Tyr 530 535 540 Ser Gln His Phe Ser Gly Arg Lys Leu Thr Trp Leu His Tyr Leu Cys 545 550 555 560 Thr Gly Glu Val Lys Met Asn Tyr Leu Gly Lys Pro Tyr Val Ala Met 565 570 575 Val Thr Thr Tyr Gln Met Ala Val Leu Leu Ala Phe Asn Asn Ser Glu 580 585 590 Thr Val Ser Tyr Lys Glu Leu Gln Asp Ser Thr Gln Met Asn Glu Lys 595 600 605 Glu Leu Thr Lys Thr Ile Lys Ser Leu Leu Asp Val Lys Met Ile Asn 610 615 620 His Asp Ser Glu Lys Glu Asp Ile Asp Ala Glu Ser Ser Phe Ser Leu 625 630 635 640 Asn Met Asn Phe Ser Ser Lys Arg Thr Lys Phe Lys Ile Thr Thr Ser 645 650 655 Met Gln Lys Asp Thr Pro Gln Glu Met Glu Gln Thr Arg Ser Ala Val 660 665 670 Asp Glu Asp Arg Lys Met Tyr Leu Gln Ala Ala Ile Val Arg Ile Met 675 680 685 Lys Ala Arg Lys Val Leu Arg His Asn Ala Leu Ile Gln Glu Val Ile 690 695 700 Ser Gln Ser Arg Ala Arg Phe Asn Pro Ser Ile Ser Met Ile Lys Lys 705 710 715 720 Cys Ile Glu Val Leu Ile Asp Lys Gln Tyr Ile Glu Arg Ser Gln Ala 725 730 735 Ser Ala Asp Glu Tyr Ser Tyr Val Ala 740 745 <210> SEQ ID NO 33 <211> LENGTH: 770 <212> TYPE: PRT <213> ORGANISM: Caenorhabditis elegans <400> SEQUENCE: 33 Cys Asp Ser Glu Val Val Trp Lys Lys Leu Gln Asp Gly Leu Asp Val 1 5 10 15 Ala Tyr Arg Arg Glu Asn Met Ala Pro Lys Asp Tyr Met Thr Leu Tyr 20 25 30 Thr Ser Val Tyr Asp Tyr Cys Thr Ser Ile Thr Leu Ser Thr Ser Arg 35 40 45 Arg Asp Gly Glu Asp Gly Arg Ala Glu Ser Ser Thr Pro Ala Arg Thr 50 55 60 Ala Gly Ala Asp Phe Val Gly His Glu Met Tyr Gln Arg Val Glu Glu 65 70 75 80 Tyr Val Lys Ala Tyr Val Ile Ala Val Cys Glu Lys Gly Ala Glu Leu 85 90 95 Ser Gly Glu Asp Leu Leu Lys Tyr Tyr Thr Thr Glu Trp Glu Asn Phe 100 105 110 Arg Ile Ser Ser Lys Val Met Asp Gly Ile Phe Ala Tyr Leu Asn Arg 115 120 125 His Trp Ile Arg Arg Glu Leu Asp Glu Gly His Glu Asn Ile Tyr Met 130 135 140 Val Tyr Thr Leu Ala Leu Val Val Trp Lys Arg Asn Leu Phe Asn Asp 145 150 155 160 Leu Lys Asp Lys Val Ile Asp Ala Met Leu Glu Leu Ile Arg Ser Glu 165 170 175 Arg Thr Gly Ser Met Ile Asn Ser Arg Tyr Ile Ser Gly Val Val Glu 180 185 190 Cys Leu Val Glu Leu Gly Val Asp Asp Ser Glu Thr Asp Ala Lys Lys 195 200 205 Asp Ala Glu Thr Lys Lys Leu Ala Val Tyr Lys Glu Phe Phe Glu Val 210 215 220 Lys Phe Leu Glu Ala Thr Arg Gly Phe Tyr Thr Gln Glu Ala Ala Asn 225 230 235 240 Phe Leu Ser Asn Gly Gly Asn Val Thr Asp Tyr Met Ile Lys Val Glu 245 250 255 Thr Arg Leu Asn Gln Glu Asp Asp Arg Cys Gln Leu Tyr Leu Asn Ser 260 265 270 Ser Thr Lys Thr Pro Leu Ala Thr Cys Cys Glu Ser Val Leu Ile Ser 275 280 285 Asn Gln Leu Asp Phe Leu Gln Arg His Phe Gly Gly Leu Leu Val Asp 290 295 300 Lys Arg Asp Asp Asp Leu Ser Arg Met Phe Lys Leu Cys Asp Arg Val 305 310 315 320 Pro Asn Gly Leu Asp Glu Leu Arg Lys Ser Leu Glu Asn His Ile Ala 325 330 335 Lys Glu Gly His Gln Ala Leu Glu Arg Val Ala Met Glu Ala Ala Thr 340 345 350 Asp Ala Lys Leu Tyr Val Lys Thr Leu Leu Glu Val His Glu Arg Tyr 355 360 365 Gln Ser Leu Val Asn Arg Ser Phe Lys Asn Glu Pro Gly Phe Met Gln 370 375 380 Ser Leu Asp Lys Ala Ala Thr Ser Phe Ile Asn Asn Asn Ala Val Thr 385 390 395 400 Lys Arg Ala Pro Pro Gln Ala Gln Leu Thr Lys Ser Ala Glu Leu Leu 405 410 415 Ala Arg Tyr Cys Asp Gln Leu Leu Arg Lys Ser Ser Lys Met Pro Asp 420 425 430 Glu Ala Glu Leu Glu Glu Leu Gln Thr Lys Ile Met Val Val Phe Lys 435 440 445 Tyr Ile Asp Asp Lys Asp Val Phe Ser Lys Phe Tyr Thr Lys Met Phe 450 455 460 Ser Lys Arg Leu Ile Ser Glu Leu Ser Ala Ser Asp Glu Ala Glu Ala 465 470 475 480 Asn Phe Ile Thr Lys Leu Lys Ser Met Cys Gly Tyr Glu Tyr Thr Ala 485 490 495 Arg Leu Ser Lys Met Val Asn Asp Thr Gln Val Ser Lys Asp Leu Thr 500 505 510 Ala Asp Phe Lys Glu Lys Lys Ala Asp Met Leu Gly Gln Lys Ser Val 515 520 525 Glu Phe Asn Val Leu Val Leu Ser Ser Gly Ser Trp Pro Thr Phe Pro 530 535 540 Thr Thr Pro Ile Thr Leu Pro Gln Gln Leu Ser Lys Thr Ile Glu Ile 545 550 555 560 Phe Gly Gln Phe Tyr Asn Glu Lys Phe Asn Gly Arg Arg Leu Thr Trp 565 570 575 Val Tyr Ser Gln Ser Arg Gly Glu Ile Thr Ser Thr Ala Phe Pro Lys 580 585 590 Lys Tyr Val Phe Thr Ala Thr Thr Ala Gln Met Cys Thr Met Leu Leu 595 600 605 Phe Asn Glu Gln Asp Ser Tyr Thr Val Glu Gln Ile Ala Ala Ala Thr 610 615 620 Lys Met Asp Glu Lys Ser Ala Pro Ala Ile Val Gly Ser Leu Ile Lys 625 630 635 640 Asn Leu Val Leu Lys Ala Asp Thr Glu Leu Gln Lys Glu Asp Glu Val 645 650 655 Pro Met Thr Ala Thr Val Ser Leu Asn Lys Ala Tyr Met Asn Lys Lys 660 665 670 Val Arg Val Asp Leu Ser Lys Phe Thr Met Lys Gln Asp Ala Val Arg 675 680 685 Asp Thr Glu Asn Val Gln Lys Asn Val Glu Glu Asp Arg Lys Ser Val 690 695 700 Ile Ser Ala Cys Ile Val Arg Ile Met Lys Thr Arg Lys Arg Val Gln 705 710 715 720 His Gln Gln Leu Met Thr Glu Val Ile Thr Gln Leu Ser Gly Arg Phe 725 730 735 Lys Pro Lys Val Glu Met Ile Lys Arg Cys Ile Gly Ser Leu Ile Glu 740 745 750 Lys Glu Tyr Met Leu Arg Thr Glu Gly Gln Lys Asp Leu Tyr Glu Tyr 755 760 765 Leu Ala 770 <210> SEQ ID NO 34 <211> LENGTH: 773 <212> TYPE: PRT <213> ORGANISM: Drosophila melanogaster <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/AAA85085 <309> DATABASE ENTRY DATE: 1996-01-03 <313> RELEVANT RESIDUES: (1)..(773) <400> SEQUENCE: 34 Met Asn Arg Ser Gly Asn Ser Gln Thr Thr Gln Lys Leu Val Asn Leu 1 5 10 15 Asp Asp Ile Trp Ser Glu Leu Val Glu Gly Ile Met Gln Val Phe Glu 20 25 30 His Glu Lys Ser Leu Thr Arg Ser Gln Tyr Met Arg Phe Tyr Thr His 35 40 45 Val Tyr Asp Tyr Cys Thr Ser Val Ser Ala Ala Pro Ser Gly Arg Ser 50 55 60 Ser Gly Lys Thr Gly Gly Ala Gln Leu Val Gly Lys Lys Leu Tyr Asp 65 70 75 80 Arg Leu Glu Gln Phe Leu Lys Ser Tyr Leu Ser Glu Leu Leu Thr Lys 85 90 95 Phe Lys Ala Ile Ser Gly Glu Glu Val Leu Leu Ser Arg Tyr Thr Lys 100 105 110 Gln Trp Lys Ser Tyr Gln Phe Ser Ser Thr Val Leu Asp Gly Ile Cys 115 120 125 Asn Tyr Leu Asn Arg Asn Trp Val Lys Arg Glu Cys Glu Glu Gly Gln 130 135 140 Lys Gly Ile Tyr Lys Ile Tyr Arg Leu Ala Leu Val Ala Trp Lys Gly 145 150 155 160 His Leu Phe Gln Val Leu Asn Glu Pro Val Thr Lys Ala Val Leu Lys 165 170 175 Ser Ile Glu Glu Glu Arg Gln Gly Lys Leu Ile Asn Arg Ser Leu Val 180 185 190 Arg Asp Val Ile Glu Cys Tyr Val Glu Leu Ser Phe Asn Glu Glu Asp 195 200 205 Thr Asp Ala Glu Gln Gln Lys Leu Ser Val Tyr Lys Gln Asn Phe Glu 210 215 220 Asn Lys Phe Ile Ala Asp Thr Ser Ala Phe Tyr Glu Lys Glu Ser Asp 225 230 235 240 Ala Phe Leu Ser Thr Asn Thr Val Thr Glu Tyr Leu Lys His Val Glu 245 250 255 Asn Arg Leu Glu Glu Glu Thr Gln Arg Arg Gly Phe Asn Ser Lys Asn 260 265 270 Gly Leu Ser Tyr Leu His Glu Thr Thr Ala Asp Val Leu Lys Ser Thr 275 280 285 Cys Glu Glu Val Leu Ile Glu Lys His Leu Lys Ile Phe His Thr Glu 290 295 300 Phe Gln Asn Leu Leu Asn Ala Asp Arg Asn Asp Asp Leu Lys Arg Met 305 310 315 320 Tyr Ser Leu Val Ala Leu Ser Ser Lys Asn Leu Thr Asp Leu Lys Ser 325 330 335 Ile Leu Glu Asn His Ile Leu His Gln Gly Thr Glu Ala Ile Ala Lys 340 345 350 Cys Cys Thr Thr Asp Ala Ala Asn Asp Pro Lys Thr Tyr Val Gln Thr 355 360 365 Ile Leu Asp Val His Lys Lys Tyr Asn Ala Leu Val Leu Thr Ala Phe 370 375 380 Asn Asn Asp Asn Gly Phe Val Ala Ala Leu Asp Lys Ala Cys Gly Lys 385 390 395 400 Phe Ile Asn Ser Asn Val Val Thr Ile Ala Asn Ser Ala Ser Lys Ser 405 410 415 Pro Glu Leu Leu Ala Lys Tyr Cys Asp Leu Leu Leu Lys Lys Ser Ser 420 425 430 Lys Asn Pro Glu Asp Lys Glu Leu Glu Asp Asn Leu Asn Gln Val Met 435 440 445 Val Val Phe Lys Tyr Ile Glu Asp Lys Asp Val Phe Gln Lys Tyr Tyr 450 455 460 Ser Lys Met Leu Ala Lys Arg Leu Val Asn His Thr Ser Ala Ser Asp 465 470 475 480 Asp Ala Glu Ala Met Met Ile Ser Lys Leu Lys Gln Thr Cys Gly Tyr 485 490 495 Glu Tyr Thr Val Lys Leu Gln Arg Met Phe Gln Asp Ile Gly Val Ser 500 505 510 Lys Asp Leu Asn Ser Tyr Phe Lys Gln Tyr Leu Ala Glu Lys Asn Leu 515 520 525 Thr Met Glu Ile Asp Phe Gly Ile Glu Val Leu Ser Ser Gly Ser Trp 530 535 540 Pro Phe Gln Leu Ser Asn Asn Phe Leu Leu Pro Ser Glu Leu Glu Arg 545 550 555 560 Ser Val Arg Gln Phe Asn Glu Phe Tyr Ala Ala Arg His Ser Gly Arg 565 570 575 Lys Leu Asn Trp Leu Tyr Gln Met Cys Lys Gly Glu Leu Ile Met Asn 580 585 590 Val Asn Arg Asn Asn Ser Ser Thr Tyr Thr Leu Gln Ala Ser Thr Phe 595 600 605 Gln Met Ser Val Leu Leu Gln Phe Asn Asp Gln Leu Ser Phe Thr Val 610 615 620 Gln Gln Leu Gln Asp Asn Thr Gln Thr Gln Gln Glu Asn Leu Ile Gln 625 630 635 640 Val Leu Gln Ile Leu Leu Lys Ala Lys Val Leu Thr Ser Ser Asp Asn 645 650 655 Glu Asn Ser Leu Thr Pro Glu Ser Thr Val Glu Leu Phe Leu Asp Tyr 660 665 670 Lys Asn Lys Lys Arg Arg Ile Asn Ile Asn Gln Pro Leu Lys Thr Glu 675 680 685 Leu Lys Val Glu Gln Glu Thr Val His Lys His Ile Glu Glu Asp Arg 690 695 700 Lys Leu Leu Ile Gln Ala Ala Ile Val Arg Ile Met Lys Met Arg Lys 705 710 715 720 Arg Leu Asn His Thr Asn Leu Ile Ser Glu Val Leu Asn Gln Leu Ser 725 730 735 Thr Arg Phe Lys Pro Lys Val Pro Val Ile Lys Lys Cys Ile Asp Ile 740 745 750 Leu Ile Glu Lys Glu Tyr Leu Glu Arg Met Glu Gly His Lys Asp Thr 755 760 765 Tyr Ser Tyr Leu Ala 770 <210> SEQ ID NO 35 <211> LENGTH: 387 <212> TYPE: PRT <213> ORGANISM: Schizosaccharomyces pombe <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Q10452 <309> DATABASE ENTRY DATE: 2003-09-15 <313> RELEVANT RESIDUES: (1)..(387) <400> SEQUENCE: 35 Met Asn His Gly Thr Lys Ile Pro Val Asp Pro Phe Arg Ile Ile Lys 1 5 10 15 Glu Thr Ala Arg Asp Gly Ser Thr Gly Glu Val Lys Gln Leu Ser Tyr 20 25 30 Thr Ser Ser Lys Val Val Gly Ser Gly Ser Phe Gly Val Val Met Gln 35 40 45 Val His Leu Ile Glu Ser Asp Ser Lys Ala Ala Ile Lys Arg Val Leu 50 55 60 Gln Asp Lys Arg Phe Lys Asn Arg Glu Leu Gln Ile Met Arg Ile Met 65 70 75 80 Lys His Pro Asn Ile Val Asp Leu Ile Ala Tyr Tyr Tyr Thr Thr Gly 85 90 95 Asp Asn Ser Asp Glu Val Tyr Leu Asn Leu Val Leu Glu Phe Met Pro 100 105 110 Glu Thr Ile Tyr Arg Ala Ser Arg Leu Tyr Thr Arg Gln Lys Leu Ser 115 120 125 Met Pro Met Leu Glu Val Lys Leu Tyr Ile Tyr Gln Leu Leu Arg Ser 130 135 140 Leu Ala Tyr Ile His Ala Ser Gly Ile Cys His Arg Asp Ile Lys Pro 145 150 155 160 Gln Asn Leu Leu Leu Asp Pro Glu Asn Gly Ile Leu Lys Leu Cys Asp 165 170 175 Phe Gly Ser Ala Lys Ile Leu Val Ala Gly Glu Pro Asn Val Ser Tyr 180 185 190 Ile Cys Ser Arg Tyr Tyr Arg Ala Pro Glu Leu Ile Phe Gly Ala Thr 195 200 205 Asp Tyr Thr His Ala Ile Asp Ile Trp Ser Thr Gly Cys Val Met Ala 210 215 220 Glu Leu Met Leu Gly His Pro Leu Phe Pro Gly Glu Ser Gly Ile Asp 225 230 235 240 Gln Leu Val Glu Ile Ile Lys Ile Leu Gly Thr Pro Ser Arg Glu Gln 245 250 255 Ile Lys Thr Met Asn Pro Asn Tyr Met Glu His Arg Phe Pro Gln Ile 260 265 270 Arg Pro Gln Pro Leu Ser Arg Val Phe Ser Arg Ser Val Pro Leu Asp 275 280 285 Ala Leu Asp Leu Leu Ser Lys Met Leu Gln Tyr Thr Pro Thr Asp Arg 290 295 300 Leu Thr Ala Ala Glu Ala Met Cys His Pro Phe Phe Asp Glu Leu Arg 305 310 315 320 Asp Pro Asn Thr Lys Leu His Asn Ser Arg Asn Pro Asp Ala Ser Pro 325 330 335 Arg His Leu Pro Glu Leu Phe Asn Phe Ser Pro Phe Glu Leu Ser Ile 340 345 350 Arg Pro Asp Leu Asn Gln Lys Leu Ile Pro Ser His Ala Arg Asp Ala 355 360 365 Leu Pro Val Lys Leu Asp Asp Phe Val Pro Ile Pro Ile His Arg Ala 370 375 380 Arg Ile Asp 385 <210> SEQ ID NO 36 <211> LENGTH: 161 <212> TYPE: PRT <213> ORGANISM: Schizosaccharomyces pombe <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: BAB62325 <309> DATABASE ENTRY DATE: 2001-08-01 <313> RELEVANT RESIDUES: (1)..(161) <400> SEQUENCE: 36 Met Ser Lys Ile Lys Leu Ile Ser Ser Asp Asn Glu Glu Phe Val Val 1 5 10 15 Asp Gln Leu Ile Ala Glu Arg Ser Met Leu Ile Lys Asn Met Leu Glu 20 25 30 Asp Val Gly Glu Ile Asn Val Pro Ile Pro Leu Pro Asn Val Ser Ser 35 40 45 Asn Val Leu Arg Lys Val Leu Glu Trp Cys Glu His His Lys Asn Asp 50 55 60 Leu Tyr Ser Gly Thr Glu Glu Glu Ser Asp Ile Arg Leu Lys Lys Ser 65 70 75 80 Thr Asp Ile Asp Glu Trp Asp Arg Lys Phe Met Ala Val Asp Gln Glu 85 90 95 Met Leu Phe Glu Ile Val Leu Ala Ser Asn Tyr Leu Asp Ile Lys Pro 100 105 110 Leu Leu Asp Thr Gly Cys Lys Thr Val Ala Asn Met Ile Arg Gly Lys 115 120 125 Ser Pro Glu Asp Ile Arg Lys Thr Phe Asn Ile Pro Asn Asp Phe Thr 130 135 140 Pro Glu Glu Glu Glu Gln Ile Arg Lys Glu Asn Glu Trp Ala Glu Asp 145 150 155 160 Arg <210> SEQ ID NO 37 <211> LENGTH: 194 <212> TYPE: PRT <213> ORGANISM: Saccharomyces cerevisiae <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/AAC49492 <309> DATABASE ENTRY DATE: 1996-10-25 <313> RELEVANT RESIDUES: (1)..(194) <400> SEQUENCE: 37 Met Val Thr Ser Asn Val Val Leu Val Ser Gly Glu Gly Glu Arg Phe 1 5 10 15 Thr Val Asp Lys Lys Ile Ala Glu Arg Ser Leu Leu Leu Lys Asn Tyr 20 25 30 Leu Asn Asp Met His Asp Ser Asn Leu Gln Asn Asn Ser Asp Ser Asp 35 40 45 Ser Asp Ser Asp Ser Glu Thr Asn His Lys Ser Lys Asp Asn Asn Asn 50 55 60 Gly Asp Asp Asp Asp Glu Asp Asp Asp Glu Ile Val Met Pro Val Pro 65 70 75 80 Asn Val Arg Ser Ser Val Leu Gln Lys Val Ile Glu Trp Ala Glu His 85 90 95 His Arg Asp Ser Asn Phe Pro Asp Glu Asp Asp Asp Asp Ser Arg Lys 100 105 110 Ser Ala Pro Val Asp Ser Trp Asp Arg Glu Phe Leu Lys Val Asp Gln 115 120 125 Glu Met Leu Tyr Glu Ile Ile Leu Ala Ala Asn Tyr Leu Asn Ile Lys 130 135 140 Pro Leu Leu Asp Ala Gly Cys Lys Val Val Ala Glu Met Ile Arg Gly 145 150 155 160 Arg Ser Pro Glu Glu Ile Arg Arg Thr Phe Asn Ile Val Asn Asp Phe 165 170 175 Thr Pro Glu Glu Glu Ala Ala Ile Arg Arg Glu Asn Glu Trp Ala Glu 180 185 190 Asp Arg <210> SEQ ID NO 38 <211> LENGTH: 194 <212> TYPE: PRT <213> ORGANISM: Saccharomyces cerevisiae <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: Genbank/AAB17500 <309> DATABASE ENTRY DATE: 1996-10-25 <313> RELEVANT RESIDUES: (1)..(194) <400> SEQUENCE: 38 Met Val Thr Ser Asn Val Val Leu Val Ser Gly Glu Gly Glu Arg Phe 1 5 10 15 Thr Val Asp Lys Lys Ile Ala Glu Arg Ser Leu Leu Leu Lys Asn Tyr 20 25 30 Leu Asn Asp Met His Asp Ser Asn Leu Gln Asn Asn Ser Asp Ser Glu 35 40 45 Ser Asp Ser Asp Ser Glu Thr Asn His Lys Ser Lys Asp Asn Asn Asn 50 55 60 Gly Asp Asp Asp Asp Glu Asp Asp Asp Glu Ile Val Met Pro Val Pro 65 70 75 80 Asn Val Arg Ser Ser Val Leu Gln Lys Val Ile Glu Trp Ala Glu His 85 90 95 His Arg Asp Ser Asn Phe Pro Asp Glu Asp Asp Asp Asp Ser Arg Lys 100 105 110 Ser Ala Pro Val Asp Ser Trp Asp Arg Glu Phe Leu Lys Val Asp Gln 115 120 125 Glu Met Leu Tyr Glu Ile Ile Leu Ala Ala Asn Tyr Leu Asn Ile Lys 130 135 140 Pro Leu Leu Asp Ala Gly Cys Lys Val Val Ala Glu Met Ile Arg Gly 145 150 155 160 Arg Ser Pro Glu Glu Ile Arg Arg Thr Phe Asn Ile Val Asn Asp Phe 165 170 175 Thr Pro Glu Glu Glu Ala Ala Ile Arg Arg Glu Asn Glu Trp Ala Glu 180 185 190 Asp Arg <210> SEQ ID NO 39 <211> LENGTH: 9 <212> TYPE: DNA <213> ORGANISM: artificial <220> FEATURE: <223> OTHER INFORMATION: Insert into coding sequence of CDC4 <400> SEQUENCE: 39 ggcgaactg 9 <210> SEQ ID NO 40 <211> LENGTH: 9 <212> TYPE: PRT <213> ORGANISM: Peptide Motif <220> FEATURE: <221> NAME/KEY: MOD_RES <222> LOCATION: (1)..(1) <223> OTHER INFORMATION: ACETYLATION <220> FEATURE: <221> NAME/KEY: DOMAIN <222> LOCATION: (1)..(9) <220> FEATURE: <221> NAME/KEY: MOD_RES <222> LOCATION: (4)..(4) <223> OTHER INFORMATION: PHOSPHORYLATION <220> FEATURE: <221> NAME/KEY: MOD_RES <222> LOCATION: (9)..(9) <223> OTHER INFORMATION: AMIDATION <400> SEQUENCE: 40 Gly Leu Leu Thr Pro Pro Gln Ser Gly 1 5 <210> SEQ ID NO 41 <211> LENGTH: 4 <212> TYPE: PRT <213> ORGANISM: Peptide Motif <220> FEATURE: <221> NAME/KEY: DOMAIN <222> LOCATION: (1)..(4) <220> FEATURE: <221> NAME/KEY: MOD_RES <222> LOCATION: (2)..(2) <223> OTHER INFORMATION: PHOSPHORYLATION <400> SEQUENCE: 41 Leu Thr Pro Pro 1 <210> SEQ ID NO 42 <211> LENGTH: 6 <212> TYPE: PRT <213> ORGANISM: Peptide Motif <220> FEATURE: <221> NAME/KEY: DOMAIN <222> LOCATION: (1)..(6) <220> FEATURE: <221> NAME/KEY: MOD_RES <222> LOCATION: (2)..(2) <223> OTHER INFORMATION: PHOSPHORYLATION <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (4)..(4) <223> OTHER INFORMATION: wherein Xaa can be any naturally occurring amino acid <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: (5)..(5) <223> OTHER INFORMATION: wherein Xaa can be any naturally occurring amino acid <220> FEATURE: <221> NAME/KEY: MOD_RES <222> LOCATION: (6)..(6) <223> OTHER INFORMATION: PHOSPHORYLATION <400> SEQUENCE: 42 Asp Ser Gly Xaa Xaa Ser 1 5 <210> SEQ ID NO 43 <211> LENGTH: 9 <212> TYPE: PRT <213> ORGANISM: Peptide Motif <220> FEATURE: <221> NAME/KEY: DOMAIN <222> LOCATION: (1)..(9) <220> FEATURE: <221> NAME/KEY: MOD_RES <222> LOCATION: (4)..(4) <223> OTHER INFORMATION: PHOSPHORYLATION <400> SEQUENCE: 43 Phe Leu Pro Thr Pro Val Leu Glu Asp 1 5 

1. An isolated binding pocket of a SCF complex or component thereof associated with substrate selection and/or orientation.
 2. An isolated binding pocket of claim 1 wherein the component is an F-box protein comprising an F-box and a WD repeat domain.
 3. Molecules or molecular complexes that comprise all or parts of one or more of a binding pocket as claimed in claim 1, or a homolog of the binding pocket that has similar structure and shape.
 4. A crystal comprising a binding pocket of an F-box protein involved in substrate selection and/or orientation.
 5. A crystal of claim 4 wherein the F box protein comprises an F box and a WD repeat domain.
 6. A crystal comprising a binding pocket of claim 1 complexed or associated with a substrate.
 7. A crystal of claim 6 wherein the ligand or substrate is a CPD motif containing protein, or part thereof.
 8. A crystal according to claim 4 having the structural coordinates shown in Table
 6. 9. A model of a binding pocket of a SCF complex using a crystal according to claim
 8. 10. A model of: (a) a binding pocket of an SCF complex of claim 1; and (b) a modification of the model of (a).
 11. A model of a binding pocket of an F-box protein of claim 2 that substantially represents the structural coordinates specified in Table
 6. 12. A binding pocket of claim 2 which comprises a WD40 repeat domain characterized by one or more of the following characteristics: (a) a 7 or 8 blade β-propeller structure, in particular a 8 blade β-propeller structure; (b) a disk like structure characterized by a cavity in the middle and two opposing circular surfaces of different size; (c) a conical frustum of about 40 Å top surface and about 50 Å bottom surface, an overall thickness of 30 Å and a central pore of 6 Å diameter; and (d) a CPD binding site on the top surface of the frustum of (c) and running across the edge, while the bottom surface of the frustum links to the F-box domain.
 13. A binding pocket of claim 2 which is characterized by one or more of the following characteristics: (i) a pThr-Pro binding pocket; (ii) a deep hydrophobic pocket that selects hydrophobic residues N-terminal to the phosphorylation site of a CPD motif, and (iii) a through space electrostatic selection against basic residues C-terminal to the phosphorylation site of a CPD motif.
 14. A binding pocket of claim 2 which comprises a helical linker characterized by a helices that form a stalk and pedestal like structure that connects and orients a WD repeat domain.
 15. A binding pocket of claim 2 as shown in FIG. 3a which is further characterized by one or more of the following: (a) a αhelix that is 30 Å in length and is anchored at its N-terminus to the hydrophobic core of an F-box/helical extension and at its C-terminus to the hydrophobic core of a WD repeat domain, (b) the helix of (a) anchored at its amino terminus to an F-box through hydrophobic interactions; (c) a second ahelix packed along the base of the helix of (a) or (b) opposite to the F-box through hydrophobic interactions; and (d) a C-terminal end of the helix of (a) inserted obliquely between propeller blades β7 and β8 of an WD40 domain through van der Wals and hydrophobic interactions.
 16. A binding pocket of claim 2 which is a CPD motif binding pocket comprising a hydrophobic pocket that surrounds the open central channel of a 7 or 8 blade WD repeat propeller.
 17. A binding pocket of claim 2 which is a Cdc4 polypeptide that interacts with a CPD motif characterized by one or more of the following: (a) a WD repeat domain surface composed of invariant and highly conserved residues from α-propeller blades; (b) a three-sided pocket formed by Trp426, Thr386, and Arg 485; (c) a three-sided pocket formed by Trp426, Thr441, Thr 465, and Arg 485; (d) a hydrophobic pocket composed of Trp 426, Trp 717, Thr 386, and Val 384, (e) a pocket formed by Leu634, Met590, and Tyr574; and (f) a pocket formed by Arg485, Arg467, Arg534, Tyr548, and Arg572.
 18. A binding pocket of claim 1 comprising one or more of the amino acid residues for an F-box protein crystal or F-box protein-substrate crystal identified in Table 3 or Table
 4. 19. A computer-readable medium having stored thereon a crystal of claim
 8. 20. A method of determining the secondary and/or tertiary structures of a polypeptide comprising the step of using a crystal of claim
 8. 21. A method of screening for a ligand capable of associating with a binding pocket and/or inhibiting or enhancing the atomic contacts of interactions in a binding pocket, comprising the use of a crystal of claim
 8. 22. A method of conducting a drug discovery business comprising: (a) providing one or more systems employing the atomic interactions, atomic contacts, or structural coordinates of a binding pocket of claim 1, to identify agents by their ability to inhibit or potentiate the atomic interactions or atomic contacts of the binding pocket; (b) conducting therapeutic profiling of agents identified in step (a), or further analogs thereof, for efficacy and toxicity in animals; and (d) formulating a pharmaceutical preparation including one or more agents identified in step (b) as having an acceptable therapeutic profile.
 23. A method for regulating an SCF complex by changing a structure of a binding pocket of claim
 1. 24. Use of a modulator of a binding pocket of claim 1 in the manufacture of a medicament to treat and/or prevent a disease in a mammalian patient.
 25. A pharmaceutical composition comprising a ligand or modulator of a binding pocket according to claim 1, and optionally a pharmaceutically acceptable carrier, diluent, excipient or adjuvant or any combination thereof. 